Nucleic acid molecule encoding abscisic acid responsive element-binding factor 2

A nucleic acid molecule encoding the Abscisic acid responsive element binding factor 2 (ABF2) was isolated and its nucleotide sequence determined. ABF2 belongs to the ABF family of factors which bind abscisic acid responsive elements in plants. Expression of ABFs is inducible by abscisic acid and various stress treatments. ABFs have the potential to activate a large number of abscisic acid/stress responsive genes and thus a nucleic acid molecule encoding ABF2 can be used to generate transgenic plants that are tolerant to multiple environmental stresses.

BACKGROUND OF THE INVENTION
 This invention relates to a family of novel transcription factors that bind
 to various abscisic acid responsive elements(ABREs), more particularily,
 factors named as ABFs(ABRE-Binding Factors) isolated by yeast one-hybrid
 screening of an Arabidopsis cDNA expression library using a prototypical
 ABRE (SEQ ID NO: 9; GGACACGTGGCG).
 Abscisic acid (ABA) is one of the major plant hormones that plays an
 important role during plant growth and development (Leung and Giraudat,
 1998). The hormone controls several physiological processes during seed
 development and germination. During vegetative growth, ABA is known to
 mediate responses to various adverse environmental conditions such as
 drought, high salt and cold/freezing (Shinozaki and Yamaguchi-Shinozaki,
 1996).
 One of the ABA-mediated responses to various environmental stresses is the
 induced expression of a large number of genes, whose gene products are
 involved in the plant's adaptation to the stresses (Ingram and Bartels,
 1996). ABA responsive elements (ABREs), i.e., cis-regulatory elements that
 mediate the ABA-modulated gene expression, have been identified from the
 promoter analysis of ABA-regulated genes (reviewed in Busk and Pages,
 1998). One class of the ABREs includes elements that share a PyACGTGGC (Py
 indicates C or T) consensus sequence, which can be considered a subset of
 a larger group of cis-elements known as "G-box" (Menkens et al., 1995).
 Another class of ABREs, known as "coupling elements (CE)" or "motif 111",
 shares a CGCGTG consensus sequence. Both classes of ABREs, here, referred
 to as G/ABRE (G-box-like ABRE) and C/ABRE (CE-like ABRE), respectively,
 are almost ubiquitous in the promoter regions of ABA responsive genes of
 both monocotyledonous and dicotyledonous plants.
 A number of basic leucine zipper (bZIP) class DNA-binding proteins are
 known to interact with the ABREs (Busk and Pages, 1998). EMBP1 and TAF1
 have been isolated based on their in vitro binding activity to G/ABREs.
 GBF3, originally identified as one of the G-box binding factors (GBFs)
 involved in the light regulation of a ribulose bisphosphate carboxylase
 gene (Schindler et al., 1992), has been cloned using the ABA-responsive,
 G-box element of a Arabidopsis Adh1 gene. Recently, a family of
 embryo-specific factors has been reported that can recognize both G/ and
 C/ABREs (Kim and Thomas, 1998; Kim et al., 1997). Other factors binding to
 G-box have also been described (Foster et al., 1994).
 Although ABRE-binding factors have been known for some time, several
 observations suggest that hitherto unidentified factors are involved in
 ABA-regulated gene expression during stress response, especially in
 vegetative tissues. ABA-induction of rice rab16A and Arabidopsis rd29B
 genes requires de novo protein synthesis (Nakagawa et al., 1996;
 Yamaguchi-Shinozaski and Shinozaki, 1994), suggesting the involvement of
 ABA-inducible factors. In vivo binding of ABA-inducible factors has been
 demonstrated in maize rab17 gene (Busk et al., 1997). In the case of
 rab16B gene, currently unknown, C/ABRE-binding factor(s) has been
 suggested to mediate ABA response through the motif III (Ono et al.,
 1996). Furthermore, it has been well established by genetic studies that
 different ABA signaling pathways operate in seeds and in vegetative
 tissues, respectively (Leung and Giraudat, 1998), and tissue-specific
 ABRE-binding activities have been demonstrated (Pla et al., 1993). None of
 the source materials used in the previous protein-DNA interaction
 clonings, however, were ABA- or stress-treated young plant tissues, and
 thus, inducible factors that may be critical for the ABA-mediated stress
 response during vegetative growth phase may have been missed so far.
 Numerous stress responsive genes involved in plant's adaptation to various
 environmental stresses are regulated by ABA through G/ABREs or C/ABREs
 (Ingram and Bartels, 1996). Therefore, overexpression of ABRE-binding
 transcription factors will result in the activation of these
 stress-inducible genes and thus enhanced stress tolerance. Hence, once
 isolated, the ABRE-binding factors will be suitable for the generation of
 transgenic plants that are tolerant to multiple environmental stresses.
 Feasibility of manipulating transcription factors for the improved stress
 tolerance has been demonstrated by others recently (Jaglo-Ottosen et al.,
 1998; Kasuga et al., 1999).
 SUMMARY OF THE INVENTION
 This invention relates to a family of novel transcription factors that bind
 to various ABREs. The factors, named as ABFs (ABRE-Binding Factors), were
 isolated by yeast one-hybrid screening of an Arabidopsis cDNA expression
 library using a prototypical ABRE (SEQ ID NO: 9; GGACACGTGGCG). ABFs are
 bZIP class transcription factors that can bind to both G/ABREs and
 C/ABREs. Expression of ABFs is inducible by ABA and various stress
 treatments, and they can transactivate an ABRE-containing reporter gene in
 yeast. Thus, ABFs have potential to activate a large number of ABA/stress
 responsive genes and thus can be used to generate transgenic plants that
 are tolerant to multiple environmental stresses.

DETAILED DESCRIPTION OF THE INVENTION
 Materials and Methods
 Plant materials--Arabidopsis thaliana (ecotype Columbia) was grown at
 22.degree. C. on pots of soil (a 1:1 mixture of vermiculite and peat moss)
 irrigated with mineral nutrient solution (0.1% Hyponex) in 8 hr light/16
 hr dark cycles. For RNA isolation, 4-5 weeks old plants were subject to
 various treatments, flash-frozen in liquid nitrogen and kept at
 -70.degree. C. until needed. For ABA treatment, roots of plants were
 submerged, after the removal of soil, in a 100 .mu.M ABA (Sigma, No A
 1012) solution for 4 hr with gentle shaking. ABA solution was also sprayed
 intermittently during the incubation period. Salt treatment was performed
 in the same way, except that 250 mM NaCl solution was employed. For
 drought treatment, plants were withheld from water for two weeks before
 harvest, and left on the bench, after removing soil, for 1 hr just before
 collection. For cold treatment, plants were placed at 4.degree. C. for 24
 hr under dim light before harvest.
 Yeast techniques, DNA manipulation and RNA gel blot analysis--Standard
 methods (Ausubel et al., 1994; Guthrie and Fink, 1991; Sambrook et al.,
 1989) were used in manipulating DNA and yeast. DNA sequencing was
 performed on ABI 310 Genetic Analyzer, according to the manufacturer's
 instruction. DNA sequence analysis was done with DNA Strider.RTM. and
 Generunr.RTM., and BLAST algorithm (Altschul et al., 1990) was used for
 database search. Multiple sequence alignment and phylogenetic tree
 construction were performed with CLUSTAL W program (Thompson et al., 1994)
 available on the web (http://www2.ebi.ac.uk/clustalw).
 RNA was isolated according to Chomczynski and Mackey (1995) and further
 purified by LiCl precipitation followed by ethanol precipitation. For RNA
 gel blot analysis, 25 .mu.g of total RNA was fractionated on 1.1%
 formaldehyde agarose gel, transferred to nylon membrane (Hybond-N+,
 Amersham) by "downward capillary transfer" method (25), and fixed using
 Stratagene's UV Crosslinker (Model 2400). Loading of equal amount of RNAs
 was confirmed by ethidium bromide staining. Hybridization was at
 42.degree. C. in 5X SSC (1X SSC is 0.15 M NaCl, 0.015 M sodium citrate),
 5X Denhardt's solution (1X Denhadt's solution is 0.02% Ficoll, 0.02% PVP,
 0.02% BSA), 1% SDS, 100 .mu.g/ml salmon sperm DNA, and 50% foramide for
 24-30 hrs. Probes were prepared from the variable regions of ABFs. After
 hybridization, filters were washed twice in 2X SSC, 0.1% SDS at room
 temperature and three times in 0.2X SSC, 0.1% SDS for 10 min each at
 65.degree. C. Exposure time was 7-8 days. RT-PCR was performed employing
 the Access RT-PCR System (Promega) using 0.5 g of total RNA according to
 the manufacturer's instruction. Amplification after the first strand cDNA
 synthesis was 45, 35, 40 and 45 cycles for ABF1, 2, 3 and 4, respectively.
 ABF primers (sequences are available upon request) were from variable
 regions between the bZIP and the conserved regions. The actin primers used
 in the control reaction was from the Arabidopsis actin-1 gene (GenBank
 Accession No., M20016). Free of contaminating DNA in RNA samples was
 confirmed by using primer sets (ABF3 and actin) that flank introns.
 cDNA library construction and yeast one-hybrid screening-Poly A(+) RNA was
 isolated from total RNAs prepared from ABA- or salt-treated Arabidopsis
 seedlings, using Qiagen's Oligotex resin. cDNA was synthesized from an
 equal mixture (6 .mu.g total) of poly A(+) RNAs prepared from the two
 sources of total RNAs employing a Stratagene's cDNA synthesis kit. cDNA
 was fractionated on a Sepharose CL-2B column, peak fractions containing
 cDNAs larger than 500 bp were pooled, and pooled cDNAs were ligated with
 pYESTrp2 (Invitrogen) predigested with Eco RI-Xho I. The ligation mixture
 was electroporated into E. coli DH10B cells. Titer of this original
 library was 5.4.times.10.sup.7 cfu. Portion of the library
 (2.times.10.sup.7) was plated on 15 cm plates at a density of 150,000
 cfu/plate. Cells were suspended in LB after overnight growth at 37.degree.
 C. on plates and pooled together. Finally, plasmid DNA was prepared from
 the collected cells.
 pYC7-I and pSK1 (Kim and Thomas, 1998) were used as HIS3 and lacZ reporter
 plasmids, respectively. The G/ABRE reporter construct was prepared by
 inserting a trimer of Em1a element (SEQ ID NO: 9; Guiltinan et al., 1990)
 into the Sma I site of pYC7-I and the Xba I site of pSK1. In order to
 prepare reporter yeast, YPH 500 was transformed with the Stu I-digested
 pYC7-I reporter construct. Resulting Ura+ colonies were transformed with
 the pSK1 construct and maintained on a SC-LEU-URA medium. Screening of the
 library was performed as described (Kim and Thomas, 1998) except that
 transformed reporter yeast was grown on Gal/Raf/CM-HIS-LEU-TRP plates
 instead of Glu/CM-HIS-LEU-TRP plates. Putative positive clones from the
 screen were streaked on fresh Gal/Raf/CM-HIS-LEU-TRP plates to purify
 colonies. After .beta.-galactosidase assay, well-isolated single colonies
 were patched on Glu/CM-LEU-TRP-URA plates to be kept as master plates.
 Galactose-dependency of the His.sup.+ /lacZ.sup.+ phenotype of the
 purified isolates was examined subsequently by comparing their growth
 pattern and .beta.-galactosidase activity on Gal/Raf/CM-HIS-LEU-TRP and
 Glu/CM-HIS-LEU-TRP dropout plates.
 Analysis of positive clones--Yeast DNA was prepared from 1.5 ml of
 overnight cultures of the positive clones. PCR was performed with primers
 derived from the pYESTrp2 vector sequences flanking the inserts (pYESTrp
 forward and reverse primers). PCR products were digested with Eco RI, Hae
 III, or Alu I in order to group the cDNAs. For library plasmid rescue,
 yeast DNAs from representative clones were introduced into DH10B E. coli
 cells by electroporation. Plasmid DNAs used in DNA sequencing and
 confirmation experiments were isolated from these E. coli transformants by
 the alkaline lysis method. For the confirmation experiment shown in FIG.
 1, plasmid DNAs thus isolated were re-introduced into the yeast containing
 pSK1 or ABRE-pSK1, transformants were kept on Glu/CM-LEU-TRP plates, and
 their growth was tested after spotting 5 .mu.l of overnight cultures (1/50
 dilutions) on Gal/Raff/CM-HIS-LEU-TRP or Glu/CM-HIS-LEU-TRP plates
 containing 2.5 mM 3-aminotriazole.
 Isolation of full-length ABF3 and 4--A PCR approach was used to isolate the
 missing 5' portions of clone 11 and clone 19. Database search revealed
 that clone 11 was part of the BAC clone F28A23 of the Arabidopsis
 chromosome IV. On the other hand, the 5' portion of the clone 19 sequence
 was identical to the 3' region of an EST clone, 176F17T7. Based on the
 sequence information, 5' PCR primers (5'-GAAGCTTGATCCTCCTAGTTGTAC-3' for
 clone 11 and 5'-ATTTGAACAAGGGTTTTAGGGC-3' for; SEQ ID NO: 16; for clone
 19) were synthesized. 3' primers (5'-TTACAATCACCCACAGAACCTGCC-3'; SEQ ID
 NO: 17 and 5'-GATTTCGTTGCCACTCTTAAG-3'; SEQ ID NO: 18, which are
 complementary to the 3'-most sequences of clones 11 and 19, respectively)
 were prepared using our sequence information. PCR was performed with Pwo
 polymerase (Boeringer Mannheim), using the primer sets and 1 .mu.g of our
 library plasmid DNA. After 30 cycles of reaction, the DNA fragments
 corresponding to the expected size of the full-length clones were
 gel-purified and cloned into the PCR-Script vector (Stratagene). Several
 clones from each PCR product were then sequenced in their entirety. The
 fidelity of the full-length sequences was confirmed by comparing their
 sequences with each other and with those of the original partial clones
 and the genomic clones deposited later by the Arabidopsis Genome
 Initiative Project.
 Plasmid constructs--In order to prepare a GST-ABF fusion constructs, entire
 coding regions and the 3' untranlated regions of ABF1 and ABF3 were
 amplified by PCR using Pfu polymerase (Stratagene). After Xho I digestion
 followed by gel-purification, the fragments were cloned into the Sma I-Sal
 I sites of pGEX-5X-2 (Pharmacia Biotech). The constructs used in
 transactivation assay were also prepared in a similar way. The coding
 regions were amplified by PCR. Resulting fragments were digested with Xho
 I, gel-purified and cloned into pYX243. pYX243 was prepared by Nco I
 digestion, Klenow fill-in reaction, Sal I digestion and gel-purification.
 Intactness of the junction sequences was confirmed by DNA sequencing.
 Preparation of recombinant ABFs and mobility shift assay--Recombinant ABF1
 and ABF3 were prepared employing a GST Purification Module from Pharmacia
 Biotech, according to the supplier's instruction. E. coli BL21 cells were
 transformed with the GST-ABF constructs by electroporation. In order to
 prepare bacterial extract, a single colony of transformed bacteria was
 inoculated in 2YT/Amp medium and grown overnight. The culture was diluted
 (1:100) into 250 ml of fresh media. IPTG was added to the culture to a
 final concentration of 0.1 mM when A.sub.600 reached 0.7. Cells were
 harvested by centrifugation after further growth (1.5 hr). The bacterial
 pellet was resuspended in 12.5 ml of PBS (0.14 M NaCl, 2.7 mM KCl, 10.1 mM
 Na.sub.2 HPO.sub.4, 1.8 mM KH.sub.2 PO.sub.4, PH7.3) and sonicated on a
 Branson Sonifier 250 (4.times.40 s burst at setting 5 at 80% duty cycle).
 The lysate was cleared of cell debris by centrifugation, and the
 supernatant was loaded onto a column packed with 0.125 ml (bed volume) of
 glutathione Sepharose 4B resin. Wash and elution was performed as
 suggested by the supplier. Protein concentration was determined using the
 BIO-RAD protein assay kit. Production of GST-ABF1 fusion protein was
 confirmed by Western blotting using GST antibody.
 Mobility shift assay was performed as described (Kim et al., 1997). To
 prepare probes, oligonucleotide sets shown in FIG. 4 were annealed by
 boiling 100 pmoles each of complementary oligonucleotides for 5 min and
 slowly cooling to room temperature. Portions of the annealed
 oligonucletides (4 pmoles of each set) were labeled by Klenow fill-in
 reaction in the presence of .sup.32 P-dATP. Binding reactions were on ice
 for 30 min, and electrophoresis was performed at 4.degree. C.
 Binding site selection assay--A pool of 58 bases oligonucleotide, R58,
 containing 18 bases of random sequence was synthesized:
 CAGTTGAGCGGATCCTGTCG(N).sub.18 GAGGCGAATTCAGTGCAACT (SEQ ID NO: 19). The
 random sequence is flanked by Bam HI and Eco RI sites for the convenience
 of cloning after selection. R58 was made double strand by annealing a
 primer, RANR, (SEQ ID NO: 20) AGTTGCACTGAATTCGCCTC, and then by extending
 it using Klenow fragment. For the first round of selection, 5 pmoles of
 the double strand R58 (P0 probe) was mixed with 5 .mu.g of the recombinant
 ABF1 in a 100 .mu.l of binding buffer (10% glycerol, 25 mM HEPES, pH 7.6,
 100 mM NaCl, 0.5 mM EDTA, 1 mM DTT) containing 4 .mu.g of poly [d(I-C)]
 and incubated on ice for 30 min. The mixture was loaded onto 0.1 ml of
 glutathione Sepharose 4B resin packed on a disposable column, washed with
 10 volumes of the binding buffer, and eluted with 0.3 ml of 10 mM
 glutathione. Bound DNA was purified by phenol/chloroform extraction
 followed by ethanol precipitation. Amplification of the selected DNA was
 performed by PCR, using 20 pmoles each of RANF SEQ ID NO: 21)
 (CAGTTGAGCGGATCCTGTCG) and RANR primers in a buffer (10 mM Tris, pH 9.0,
 50 mM KCl, 0.1% Triton X-100, 2.5 mM MgCl.sub.2) containing 150 .mu.M
 dNTP-dATP, 4 .mu.M dATP, 10 .mu.Ci of .sup.32 P-dATP. Reaction was carried
 out 20 cycles (10 sec, 94.degree. C./10 sec, 50.degree. C./1 min,
 72.degree. C.). Amplified DNA was purified on a polyacrylamide gel, the
 band was excised after autoradiography, and DNA was eluted by standard
 method to be used as a probe DNA for the next round of selection. The
 selection cycle was repeated two more times. For the fourth and the fifth
 rounds of selection, bound DNAs were isolated after EMSA, by eluting DNA
 from the dried gel fragment containing the shifted bands. The amplified
 DNA (P5 probe) from the last selection was cloned into pBluescript
 (Stratagene) after Eco RI and Bam HI digestion, and plasmid DNAs from 50
 random colonies were sequenced.
 Transactivation assay--Reporter yeast containing the lacZ reporter gene
 (pYC7-1) with or without the ABRE was transformed with various pYX243/ABF
 constructs, and transformants were kept on Glu/CM-LEU-URA plates. For the
 assay, 5 colonies from each transformant group were grown in a
 Glu/CM-LEU-URA medium overnight to A.sub.600 of approximately 1. The
 cultures were diluted 4-6 times with fresh media, grown further for 3 hr,
 and pelleted by brief centrifugation. The cells were washed twice with
 Gal/Raf/CM-LEU-URA medium, resuspended in 4 ml of the same medium, and
 grown for 4 hr to induce the expression of ABFs. A.sub.600 was measured at
 the end of the growth period, and 0.5 ml aliquots of the culture, in
 duplicates, were pelleted. The pellets were resuspended in 0.665 ml of H
 buffer (100 mM HEPES, 150 mM NaCl, 2 mM MgCl.sub.2, 1% BSA, pH 7.0) and
 permeabilized by vortexing for 1 min after the addition of 0.055 ml each
 of CHCl.sub.3 and 0.1% SDS. The reaction was started by adding 0.125 ml of
 40 mM stock solution of CPRG (chlorophenylred-b-D-galactopyranoside) and
 incubation was continued at 30.degree. C. until the color changed to red.
 Reactions were stopped by the addition of 0.4 ml of 1 M Na.sub.2 CO.sub.3.
 The mixtures were microfuged for 5 min to remove cell debris and A.sub.574
 was measured. .beta.-galactosidase activity was expressed in Miller units.
 Results
 Isolation of ABE-binding protein factors--We employed a modified yeast
 one-hybrid system (Kim and Thomas, 1998; Kim et al., 1997) in order to
 isolate ABRE-binding factor(s) using the prototypical ABRE, Emla element
 (SEQ ID NO: 9; GGACACACGTGGCG). A cDNA expression library representing
 2.times.10.sup.7 cfu was constructed in a yeast expression vector
 pYESTrp2, using a mixture of equal amounts of mRNAs isolated from ABA- and
 salt-treated Arabidopsis plants. The vector contains B42 activation domain
 (Ma and Ptashne, 1987) whose expression is under the control of yeast GAL1
 promoter. Thus, expression of cDNAs, which are inserted as a fusion to the
 activation domain, is inducible by galactose and repressed by glucose. The
 library DNA was used to transform a reporter yeast that harbors the
 ABRE-containing HIS3 and lacZ reporters. From a screen of 4 million yeast
 transformants, ca. 40 His.sup.+ blue colonies were obtained, among which
 19 isolates were characterized further. Analysis of the cDNA inserts of
 the positive clones indicated that they could be divided into 4 different
 groups according to their restriction patterns. Representative clones with
 longer inserts from each group were analyzed in more detail.
 First, binding of the cDNA clones to the G/ABRE in yeast was confirmed. The
 G/ABRE-HIS3 reporter yeast was re-transformed with the library plasmid
 DNAs isolated from the representative clones. Growth pattern of the
 transformants on media lacking histidine was then examined to measure the
 HIS3 reporter activity. The result in FIG. 1 showed that transformants
 obtained with all four clones could grow on a galactose medium lacking
 histidine, but not on a glucose medium. In the same assay, the transformed
 yeast containing a control reporter construct lacking the ABRE could not
 grow on the same galactose medium. Thus, the clones could activate HIS3
 reporter gene reproducibly, indicating that they bind to the ABRE in
 yeast.
 Next, nucleotide and deduced amino acid sequences of the representative
 clones were determined. Clone 1, which represents two isolates, contained
 a cDNA insert of 1578 bp including a poly A(+) tail (FIG. 2A, SEQ ID NO.
 1). An open reading frame (ORF) that is in frame with the B42 domain was
 present within the sequence. The ORF, referred to as ABF1 (ABRE-Binding
 Factor 1), contains an ATG initiation codon near the B42-cDNA junction,
 suggesting that it is a full-length clone. The amino acid sequence
 starting from the initiation codon is shown in FIG. 2A (SEQ ID NO. 2). The
 insert of clone 2, which represents 8 isolates, is 1654 bp long (FIG. 2B,
 SEQ ID NO. 3) and the longest ORF including an initiation codon near the
 B42-cDNA junction encodes a protein of 416 amino acids (ABF2) (FIG. 2B,
 SEQ ID NO. 4).
 The insert of clone 11, representing 6 isolates, encoded a protein
 containing 434 amino acids. An ORF containing 366 amino acids was found in
 clone 19 cDNA. The clones were partial, however, and the missing 5'
 portions were isolated using the available partial sequence information on
 databases (Materials and methods). Sequencing of the full-length clones
 (FIGS. 2C and 2D, SEQ ID NOs. 5 and 7) showed that the original clone 11
 was missing the first 20 amino acids, and thus, full-length clone 11
 encodes a protein containing 454 amino acids (ABF3) (FIG. 2C, SEQ ID NO.
 6). The longest ORF of clone 19 is composed of 431 amino acids (ABF4)
 (FIG. 2D, SEQ ID NO. 8).
 ABFs are bZIP proteins--Analysis of the deduced amino acid sequence of ABF1
 revealed that it has a basic region near its C-terminus (SEQ ID NO: 2;
 FIGS. 2A and 3). The region immediately downstream of it contains 4 heptad
 repeats of leucine, indicating that ABF1 is a bZIP protein (Landshulz et
 al., 1988). Similarly, other ABFs also have a basic region followed by a
 leucine repeat region (SEQ ID NO: 4, SEQ ID NO: 6, SEQ ID NO: 8; FIGS.
 2B-D and 3). The basic regions of ABF1 and ABF3 (SEQ ID NO: 2, SEQ ID NO:
 6, respectively) are identical to each other, and those of ABF 2 and (SEQ
 ID NO: 4, SEQ ID NO: 8, respectively) are also identical (FIG. 3). The
 two, shared basic regions are same except that one of the lysine residues
 of ABF1 and ABF3 is replaced by arginine in ABF2 and ABF4. The analysis
 shows that a family of bZIP proteins with conserved basic regions
 interacts with the G/ABRE.
 ABFs also share several highly conserved regions outside the basic domains.
 As shown in FIG. 3, the conserved regions are clustered in the N-terminal
 halves. Invariably, they contain one or two potential phosphorylation
 sites. The N-most region, for example, contains one multifunctional
 calmodulin-dependent protein kinase II (CaMK II) site (X-R-X-X-S*-X) (Kemp
 and Pearson, 1990) followed by a caseine kinase II (CKII) phosphorylation
 site (X-S/T*-X-X-D/E-X). One or two CaMK II or CK II phosphorylation sites
 are also present in other conserved regions. The middle portions of ABFs
 are highly variable and rich in glutamine commonly found in
 transcriptional activation domains.
 In vitro binding activity of ABFs--In order to test in vitro DNA-binding
 activity of ABFs, we performed electrophoretic mobility shift assay (EMSA)
 using recombinant ABF1 or ABF3 and probe DNAs containing a G/ or C/ABRE.
 Similar results were obtained with both proteins and the assay result of
 ABF1 is shown in FIG. 4. A major shifted band was observed, with a weaker
 minor band (FIG. 4A, lane 2). Addition of excess, increasing amount of
 unlabeled probe DNA to the reaction mixture (lanes 3 and 4) gradually
 abolished the binding, whereas the same amount of a mutated
 oligonucleotide (lanes 5 and 6) did not. Thus, ABF1 and ABF3 exhibited
 sequence-specific binding activity to the G/ABRE in vitro.
 ABFs are similar to the Dc3 promoter-binding factors (DPBFs) (Kim and
 Thomas, 1998; Kim et al., 1997) in their basic regions (see Discussion).
 Since DPBFs are known to interact not only with a G/ABRE but also with
 C/ABREs, we tested whether ABFs can interact with C/ABREs. To date, no
 transcriptional activators interacting with the element were reported
 except the embryo-specific DPBFs. An oligonucleotide, hex-3 (SEQ ID NO:
 13; Lam and Chua, 1991), containing the C/ABRE core sequence (CGCGTG), was
 employed as a probe in an EMSA. As shown in FIG. 4B, a shifted band was
 observed (lane 2). The band formation was abolished by the addition of
 excess amounts of the cold probe DNA to the reaction mixture (lanes 3 and
 4). The competition was not observed with a mutated probe DNA (lanes 5 and
 6), demonstrating that the binding was specific to the C/ABRE. Thus, ABF1
 and ABF3 could bind to a C/ABRE as well.
 Binding site preference of ABF1--Our in vitro binding assay indicated that
 ABF1 and ABF3 can interact with both G/ and C/ABREs, although mutual
 competition assay (not shown) showed that they have higher affinity to the
 G/ABRE. In order to investigate ABF binding sites further, we performed a
 random binding site selection assay (RBSA) (Pollock and Treisman, 1990)
 (Materials and methods), using the recombinant ABF1. Shifted bands were
 visible on a mobility shift assay gel after three rounds of selection
 (FIG. 5A, top panel). After confirming the binding of ABF1 to the probe
 DNAs from the final round of selection (FIG. 5A, bottom panel) the DNA
 were cloned and sequenced.
 The 44 selected sequences are presented in FIG. 5B. The sequences could be
 divided into 4 groups (groups IA, IAA, IB, and II) according to their
 consensus sequences. All of the group I sequences, except one (sequence
 no. 49), contain an ACGT element, while the group II sequences contain the
 C/ABRE core. The most frequently selected sequences (30 of 44) are those
 sharing a strong G/ABRE, CACGTGGC (Busk and Pages, 1998): gACACGTGGC (SEQ
 ID NO: 22; group IA) or CCACGTGGC (group IAA). The group IAA element is
 similar to the prototypical ABRE, Em1a (SEQ ID NO: 9; GGACACGTGGC), while
 the group IAA consensus is the same as the palindromic G/ABREs present in
 many ABA-inducible genes such as maize rab28, Arabidopsis kin1, cor6.6 and
 Adh1 genes (reviewed in Thomas et al 1997). In some of the group IA
 sequences (sequence no. 38, 45 and 42), the GGC following the ACGT core is
 replaced by GTC, forming another palindromic consensus sequence GACACGTGTC
 (SEQ ID NO: 23). The group IB sequences share a GNTGACGTGGC (SEQ ID NO:
 24) consensus or its variants differing in one or two bases flanking the
 ACGT core. Although the conserved element differs from those of group IA
 and IAA in the bases preceding the ACGT core, it contains the same
 ACGTG(G/t)C. Hence, the preferred binding sites of ABF1 can be represented
 as ACGTG(G/t)C, with AC, CC or TG preceding it.
 One of the selected sequences (no.24 of group II) contains the C/ABRE core
 sequence (CGCGTG). The three other group II sequences also contain the
 C/ABRE core. The element in them, however, is flanked by one of the group
 I consensus sequences, and thus, they contain both types of ABREs. Another
 sequence (no. 49 of group IB) does not contains the ACGT core; the C of
 the ACGT is replaced by A. The resulting AAGTGGA sequence is similar to
 the half G-box (CCAAGTGG) of Arabidopsis Adh1 promoter, which is required
 for high level ABA-induction of the gene (de Bruxelles et al., 1996).
 Thus, ABF1 interacts with sequences without the ACGT core, which includes
 the C/ABRE. The low selection frequency, however, suggests that ABF1's
 affinity to them is lower.
 Expression of ABFs is ABA-inducible--Since we are interested in
 ABA-inducible stress responsive factors, we investigated ABA-inducibility
 of ABF expression, by RNA gel blot analysis (FIG. 6A). With the ABF1
 probe, no hybridization signal was detectable with RNA isolated from
 untreated plants, while a clear signal was detected with RNA from
 ABA-treated plants. Similar results were obtained with other ABF probes;
 while hybridization signals were weak (ABF2 and 4) or undetectable (ABF-3)
 with the RNA from untreated plants, distinct signals were observed with
 the RNA sample from ABA-treated plants. Thus, expression of ABFs is
 ABA-inducible.
 Although all are induced by ABA, the time course of ABA-induced expression
 of ABFs was not identical to each other (FIG. 6B). ABF1 RNA level reached
 a peak approximately 2 hours after ABA treatment started, remained same up
 to 12 hours and decreased to the uninduced level after 16 hours. ABF2 and
 ABF4 expression appeared to be induced faster, reaching a plateau after 30
 min of ABA treatment. Afterwards, their RNA level remained relatively same
 until 24 hour. The induction pattern of ABF3 was similar to those of ABF2
 and ABF4 except that it reached the peak level later, i.e., after 2 hours.
 We also examined the effect of various environmental stresses on the
 expression of ABFs. The results (FIG. 6A) showed that expression of ABF1
 was induced by cold treatment, but not by other stress treatments. With
 the same RNA samples, ABF2 and ABF3, on the other hand, were not induced
 by cold, but by high salt treatment. ABF4 expression was induced by all
 three treatments, although induction level after cold treatment was
 relatively low. Expression of ABFs is, thus, inducible also by various
 environmental stresses and their induction patterns are differential,
 suggesting that they function in different stress responsive pathways.
 ABFs can transactivate an ABRE-containing reporter gene in yeast--Our
 result so far demonstrated that ABF1, and probably other ABFs too, can
 bind to various ABREs and that their expression is both ABA- and
 stress-dependent. Thus, ABFs have potential to activate a large number of
 ABA/stress responsive genes, if they have transactivation capability. We
 therefore investigated whether ABFs can activate an ABRE-containing
 reporter gene. Coding regions of ABFs were cloned into a yeast expression
 vector and the constructs were individually introduced into a yeast strain
 that harbored a G/ABRE-containing lacZ reporter gene integrated into the
 chromosome. Subsequently, reporter enzyme activity was measured.
 With the ABF1 construct, .beta.-galactosidase activity was 6 times higher
 than that obtained with the control construct (FIG. 7, top panel). No
 enzyme activity was detectable with the same ABF1 construct when a
 reporter lacking the ABRE was used. Thus, ABF1 can transactivate the
 reporter gene and the activation is ABRE-dependent. With the ABF2
 construct, reporter enzyme activity two times higher than the background
 activity was detected, indicating that the factor also can transactivate
 the reporter gene (FIG. 7, top panel). Likewise, ABF3 and 4 could
 transactivate the reporter gene (FIG. 7, bottom panel). The activation
 level of ABF3 was higher than the ABF1's, while ABF4 showed weaker
 activation. The result of our transactivation assay demonstrates that ABFs
 can activate an ABRE-containing gene in yeast.
 Discussion
 Numerous studies, both genetic and biochemical, show that ABA mediates
 stress response in vegetative tissues, although not all stress responses
 are ABA-dependent (Leung and Giraudat, 1998; Shinozaki and
 Yamaguchi-Shinozaki, 1996; Thomashow, 1998; Ingram and Bartels, 1996).
 Central to the response is the ABA-regulation of gene expression through
 G/ABREs or C/ABREs. Transcription factors mediating ABA-independent cold
 and drought responses have been reported recently (Jaglo-Ottosen et al.,
 1998; Liu et al., 1998). However, those regulating ABA-dependent stress
 response via the G/ or the C/ABREs have yet to be identified. Among the
 ABRE-binding factors mentioned earlier, TAF-1 is known not to be directly
 involved in ABA responsive gene expression (Oeda et al., 1991), while
 EmBP-1 and DPBFs are highly embryo-specific (Kim and Thomas, 1998; Hollung
 et al., 1997). GBF3 and a homology-based cloned factor OSBZ8, although
 inducible by ABA, are from cultured cells or from embryos (Lu et al.,
 1996; Nakagawa et al., 1996). Taken together with the lack of data
 demonstrating their role in ABA or stress response, it is likely that
 unknown factors may mediate ABA-responsive gene expression in vegetative
 tissues.
 In a search for such transcription factors, we isolated a family of
 G/ABRE-binding proteins from young Arabidopsis plants treated with ABA or
 high salt. The factors, referred to as ABFs, are ABA/stress-inducible bZIP
 class transcription factors with shared basic regions. Sequence comparison
 with known ABRE-binding factors indicated that, although they do not show
 any significant homology to other factors, they are similar to the Dc3
 promoter-binding factors (DPBFs) (Kim and Thomas, 1998; Kim et al., 1997).
 DPBFs have been isolated from a seed-specific library based on their
 interaction with a lea gene promoter containing both G/ and C/ABREs. The
 two family members are nearly identical in their basic regions (FIG. 8A),
 and their DNA-binding properties are similar in that they can interact
 with both types of ABREs. Some of the conserved phosphorylation sites
 within the N-terminal halves of ABFs are also conserved in DPBFs. However,
 ABFs diverge from the DPBFs outside the basic regions and their immediate
 flanking sequences, overall identity being in the range of 30-40%. As a
 result, they form a subfamily distinct from DPBFs and also from other
 known factors, as shown in FIG. 8B. Furthermore, their expression patterns
 are different from those of DPBFs; i.e., DPBFs' expression is
 embryo-specific. Cloning of ABFs shows that two related subfamilies of
 ABRE-binding factors are present in seed and in vegetative tissues,
 respectively. The presence of distinct factors in the tissues that have
 similar ABRE-binding affinity has been demonstrated in maize (Pla et al.,
 1993).
 ABFs contain regions highly conserved among them apart from the basic
 regions. Thus, ABFs appear to share some properties other than DNA-binding
 activity. The conserved regions, however, do not have any easily
 recognizable motifs except that two of them can form .alpha.-helix, and
 thus, their function remains to be identified. They may be involved in
 nuclear translocation, DNA-binding, transcriptional activation, or
 interaction with other regulatory proteins. Whatever their function may
 be, the conservation of potential phosphorylation sites within the regions
 suggests that it is probably modulated by post-translational modification.
 Our in vitro binding assay showed that the most preferred binding site of
 ABF1 in vitro can be represented as CACGTGGC (FIG. 5B). The element, first
 identified as EmBP-1 recognition site (Guiltinan et al., 1990), are highly
 conserved among ABA/stress inducible promoters and strongly affect
 ABA-inducibility in vivo (Busk and Pages, 1998). Together with the fact
 that ABF1 is ABA/stress-inducible and has transcriptional activity, this
 suggests that ABF1 can potentially activate a large number of ABA/stress
 responsive genes. Also, ABF1 can bind to other ABREs including the
 C/ABREs, further supporting the broad spectrum of potential ABF1 target
 genes. The affinity to C/ABREs, however, was relatively low in vitro.
 The expression pattern of ABFs suggests that each ABF is likely to be
 involved in different stress signaling pathways. Although all are
 ABA-inducible and can bind to same ABREs, they are differentially
 regulated by various environmental stresses. ABF1 expression is induced by
 cold, ABF 2 and ABF3 by high salt, and ABF4 by cold, high salt and
 drought. The simplest interpretation of the result would be that ABF1 is
 involved in cold signal transduction, while ABF2 and ABF3 function in
 osmotic stress signaling. ABF4, on the other hand, appears to participate
 in multiple stress responses. In addition, ABFs differ in their ABA
 induction patterns. Expression of ABF1 was induced rather slowly (FIG. 6B)
 and the accumulation of its RNA was transient, while induction of other
 ABFs appeared faster and their RNA levels remained relatively stable once
 reached a plateau. The multiplicity of ABA-dependent stress signaling
 pathways has been demonstrated in Arabidopsis by genetic analysis (Leung
 and Giraudat, 1998; Ishitani et al., 1997). Our result suggests further
 that multiple transcription factors are likely to function in these signal
 transduction cascades through common ABREs.
 ABA-dependent stress responsive gene expression is critical to plant growth
 and productivity. Here, we reported a family of transcription factors that
 interact with cis-regulatory elements mediating this process. Although
 their specific roles in planta remains to be determined, our data
 presented here suggest that they are likely to be involved in various
 ABA-mediated stress responses. They can bind to ABREs highly conserved
 among stress responsive promoters. They can transactivate an
 ABRE-containing reporter gene. Their expression is induced by ABA and by
 various environmental stresses. Hence, ABFs are excellent targets of
 genetic manipulation for the generation of stress tolerant transgenic
 plants.
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 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 5
 gaagcttgat cctcctagtt gtacgaaagc ttgagtaatg gggtctagat taaacttcaa 60
 gagctttgtt gatggtgtga gtgagcagca gccaacggtg gggactagtc ttccattgac 120
 taggcagaac tctgtgttct cgttaacctt tgatgagttt cagaactcat ggggtggtgg 180
 aattgggaaa gattttgggt ctatgaacat ggatgagctc ttgaagaaca tttggactgc 240
 agaggaaagt cattcaatga tgggaaacaa taccagttac accaacatca gcaatggtaa 300
 tagtggaaac actgttatta acggcggtgg taacaacatt ggtgggttag ctgttggtgt 360
 gggaggagaa agtggtggtt ttttcactgg tgggagtttg cagagacaag gttcacttac 420
 cttgcctcgg acgattagtc agaaaagggt tgatgatgtc tggaaggagc tgatgaagga 480
 ggatgacatt ggaaatggtg ttgttaatgg tgggacaagc ggaattccgc agaggcaaca 540
 aacgctggga gagatgactt tggaggagtt tttggtcagg gctggtgtgg ttagggaaga 600
 acctcaaccg gtggagagtg taactaactt caatggcgga ttctatggat ttggcagtaa 660
 tggaggtctt gggacagcta gtaatgggtt tgttgcaaac caacctcaag atttgtcagg 720
 aaatggagta gcggtgagac aggatctgct gactgctcaa actcagccac tacagatgca 780
 gcagccacag atggtgcagc agccacagat ggtgcagcag ccgcaacaac tgatacagac 840
 gcaggagagg ccttttccca aacagaccac tatagcattt tccaacactg ttgatgtggt 900
 taaccgttct caacctgcaa cacagtgcca ggaagtgaag ccttcaatac ttggaattca 960
 taaccatcct atgaacaaca atctactgca agctgtcgat tttaaaacag gagtaacggt 1020
 tgcagcagta tctcctggaa gccagatgtc acctgatctg actccaaaga gcgccctgga 1080
 tgcatctttg tcccctgttc cttacatgtt tgggcgagtg agaaaaacag gtgcagttct 1140
 ggagaaagtg attgagagaa ggcaaaaaag gatgataaag aatagggaat cagctgcaag 1200
 atcccgcgct cgcaagcaag cttatacgat ggaactggaa gcagaaattg cgcaactcaa 1260
 agaattgaat gaagagttgc agaagaaaca agttgaaatc atggaaaagc agaaaaatca 1320
 gcttctggag cctctgcgcc agccatgggg aatgggatgc aaaaggcaat gcttgcgaag 1380
 gacattgacg ggtccctggt agagcttata atggcgtcta aggaacccaa caaagcgccg 1440
 aagttataga acaactcaga agatagaaag ctagctttgt acgtagttta ggcaggttct 1500
 gtgggtgatt gtaaatcttg aagtgtggcg gatttgacag agatagataa acacatatct 1560
 gttctatttt cctaaatctt ttggttttat cttcctgatg taatggatct ttatcatttg 1620
 tcttgaacat ctttgtgact taaccagagt gaatttatct tgtatctaaa aaaaaaaaaa 1680
 aaaaa 1685
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 6
 &lt;211&gt; LENGTH: 454
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 6
 Met Gly Ser Arg Leu Asn Phe Lys Ser Phe Val Asp Gly Val Ser Glu
 1 5 10 15
 Gln Gln Pro Thr Val Gly Thr Ser Leu Pro Leu Thr Arg Gln Asn Ser
 20 25 30
 Val Phe Ser Leu Thr Phe Asp Glu Phe Gln Asn Ser Trp Gly Gly Gly
 35 40 45
 Ile Gly Lys Asp Phe Gly Ser Met Asn Met Asp Glu Leu Leu Lys Asn
 50 55 60
 Ile Trp Thr Ala Glu Glu Ser His Ser Met Met Gly Asn Asn Thr Ser
 65 70 75 80
 Tyr Thr Asn Ile Ser Asn Gly Asn Ser Gly Asn Thr Val Ile Asn Gly
 85 90 95
 Gly Gly Asn Asn Ile Gly Gly Leu Ala Val Gly Val Gly Gly Glu Ser
 100 105 110
 Gly Gly Phe Phe Thr Gly Gly Ser Leu Gln Arg Gln Gly Ser Leu Thr
 115 120 125
 Leu Pro Arg Thr Ile Ser Gln Lys Arg Val Asp Asp Val Trp Lys Glu
 130 135 140
 Leu Met Lys Glu Asp Asp Ile Gly Asn Gly Val Val Asn Gly Gly Thr
 145 150 155 160
 Ser Gly Ile Pro Gln Arg Gln Gln Thr Leu Gly Glu Met Thr Leu Glu
 165 170 175
 Glu Phe Leu Val Arg Ala Gly Val Val Arg Glu Glu Pro Gln Pro Val
 180 185 190
 Glu Ser Val Thr Asn Phe Asn Gly Gly Phe Tyr Gly Phe Gly Ser Asn
 195 200 205
 Gly Gly Leu Gly Thr Ala Ser Asn Gly Phe Val Ala Asn Gln Pro Gln
 210 215 220
 Asp Leu Ser Gly Asn Gly Val Ala Val Arg Gln Asp Leu Leu Thr Ala
 225 230 235 240
 Gln Thr Gln Pro Leu Gln Met Gln Gln Pro Gln Met Val Gln Gln Pro
 245 250 255
 Gln Met Val Gln Gln Pro Gln Gln Leu Ile Gln Thr Gln Glu Arg Pro
 260 265 270
 Phe Pro Lys Gln Thr Thr Ile Ala Phe Ser Asn Thr Val Asp Val Val
 275 280 285
 Asn Arg Ser Gln Pro Ala Thr Gln Cys Gln Glu Val Lys Pro Ser Ile
 290 295 300
 Leu Gly Ile His Asn His Pro Met Asn Asn Asn Leu Leu Gln Ala Val
 305 310 315 320
 Asp Phe Lys Thr Gly Val Thr Val Ala Ala Val Ser Pro Gly Ser Gln
 325 330 335
 Met Ser Pro Asp Leu Thr Pro Lys Ser Ala Leu Asp Ala Ser Leu Ser
 340 345 350
 Pro Val Pro Tyr Met Phe Gly Arg Val Arg Lys Thr Gly Ala Val Leu
 355 360 365
 Glu Lys Val Ile Glu Arg Arg Gln Lys Arg Met Ile Lys Asn Arg Glu
 370 375 380
 Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Met Glu Leu
 385 390 395 400
 Glu Ala Glu Ile Ala Gln Leu Lys Glu Leu Asn Glu Glu Leu Gln Lys
 405 410 415
 Lys Gln Val Glu Ile Met Glu Lys Gln Lys Asn Gln Leu Leu Glu Pro
 420 425 430
 Leu Arg Gln Pro Trp Gly Met Gly Cys Lys Arg Gln Cys Leu Arg Arg
 435 440 445
 Thr Leu Thr Gly Pro Trp
 450
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 7
 &lt;211&gt; LENGTH: 1737
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 7
 gaacaagggt tttagggctt ggatgctttg ttttcattga aaaagaagta gaaggagtgt 60
 atacaaggat tatgggaact cacatcaatt tcaacaactt aggaggtggt ggtcatcctg 120
 gaggggaagg gagtagtaac cagatgaagc caacgggtag tgtcatgccc ttggctaggc 180
 agtcctcggt ctactccctt acctttgatg agttacagaa cacactaggt ggaccgggaa 240
 aagatttcgg gtcgatgaac atggatgaac tcctgaagag catatggact gctgaggaag 300
 ctcaggccat ggccatgact tctgcgccag ctgctacagc ggtagcgcaa cctggtgctg 360
 gtatcccacc cccaggtggg aatctccaga ggcaaggttc gttgacgttg cctagaacaa 420
 ttagtcagaa gactgttgat gaggtgtgga aatgtttgat caccaaggat ggtaatatgg 480
 aaggtagcag cggaggcggt ggtgagtcga atgtgcctcc tggaaggcaa cagactttag 540
 gggaaatgac acttgaagaa tttctgttcc gtgctggggt tgtaagagaa gataactgtg 600
 ttcaacagat gggtcaggtc aacggaaaca ataacaatgg gttttatggt aacagcactg 660
 ctgctggcgg cttaggtttt ggatttggtc agccaaatca aaacagcata acattcaatg 720
 gtactaatga ttctatgatc ttgaatcagc cacctggttt agggctcaaa atgggtggaa 780
 caatgcagca gcaacaacaa caacagcagt tgcttcagca gcaacaacag cagatgcagc 840
 agctgaatca gcctcatcca cagcagcggc tgcctcaaac catttttcct aaacaagcaa 900
 acgtagcatt ttctgcgcct gtgaatataa ccaacaaggg ttttgctggg gctgcaaata 960
 attctatcaa caataataat ggattagcta gttacggagg aaccggggtc actgttgcag 1020
 caacttctcc aggaacaagc agcgcagaaa ataattcttt atcaccagtt ccgtatgtgc 1080
 ttaatcgagg acgaagaagc aatacaggtc tagagaaggt tatcgagagg aggcaaagga 1140
 gaatgatcaa gaatcgggaa tcagctgcta gatcaagagc tcgaaagcag gcttatacat 1200
 tggaactgga agccgaaatt gaaaagctca agaaaacgaa tcaagaactg cagaaaaaac 1260
 aggctgaaat ggtggaaatg cagaagaatg agctgaaaga aacgtcgaag cgaccgtggg 1320
 gcagcaaaag gcaatgcttg agaaggacat taaccggacc atggtgaagg atgaagcaac 1380
 aagaacggat gaaccagact cctagcttgg gattaatgta ataggatagt gctacctgta 1440
 caggagatta agagaaattg agtgaaagat ctaggttaca gagtaggaga gagttttcat 1500
 tatgaataaa tgacattttg tgccctgacc tttgttagtt taggtttaga ttatcctctg 1560
 ttattgactt attgtgcttt ctggttgtta gggtttctaa aagacatagt tgtttatata 1620
 tatgtctgac tttgtattcc ggatttggtt ctcttgtgtc attaacttgg gtttagccat 1680
 tattacttaa gagtggcaac gaaatcaaaa aaaaaaaaaa aaaaaaaaaa aaaaaaa 1737
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 8
 &lt;211&gt; LENGTH: 431
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 8
 Met Gly Thr His Ile Asn Phe Asn Asn Leu Gly Gly Gly Gly His Pro
 1 5 10 15
 Gly Gly Glu Gly Ser Ser Asn Gln Met Lys Pro Thr Gly Ser Val Met
 20 25 30
 Pro Leu Ala Arg Gln Ser Ser Val Tyr Ser Leu Thr Phe Asp Glu Leu
 35 40 45
 Gln Asn Thr Leu Gly Gly Pro Gly Lys Asp Phe Gly Ser Met Asn Met
 50 55 60
 Asp Glu Leu Leu Lys Ser Ile Trp Thr Ala Glu Glu Ala Gln Ala Met
 65 70 75 80
 Ala Met Thr Ser Ala Pro Ala Ala Thr Ala Val Ala Gln Pro Gly Ala
 85 90 95
 Gly Ile Pro Pro Pro Gly Gly Asn Leu Gln Arg Gln Gly Ser Leu Thr
 100 105 110
 Leu Pro Arg Thr Ile Ser Gln Lys Thr Val Asp Glu Val Trp Lys Cys
 115 120 125
 Leu Ile Thr Lys Asp Gly Asn Met Glu Gly Ser Ser Gly Gly Gly Gly
 130 135 140
 Glu Ser Asn Val Pro Pro Gly Arg Gln Gln Thr Leu Gly Glu Met Thr
 145 150 155 160
 Leu Glu Glu Phe Leu Phe Arg Ala Gly Val Val Arg Glu Asp Asn Cys
 165 170 175
 Val Gln Gln Met Gly Gln Val Asn Gly Asn Asn Asn Asn Gly Phe Tyr
 180 185 190
 Gly Asn Ser Thr Ala Ala Gly Gly Leu Gly Phe Gly Phe Gly Gln Pro
 195 200 205
 Asn Gln Asn Ser Ile Thr Phe Asn Gly Thr Asn Asp Ser Met Ile Leu
 210 215 220
 Asn Gln Pro Pro Gly Leu Gly Leu Lys Met Gly Gly Thr Met Gln Gln
 225 230 235 240
 Gln Gln Gln Gln Gln Gln Leu Leu Gln Gln Gln Gln Gln Gln Met Gln
 245 250 255
 Gln Leu Asn Gln Pro His Pro Gln Gln Arg Leu Pro Gln Thr Ile Phe
 260 265 270
 Pro Lys Gln Ala Asn Val Ala Phe Ser Ala Pro Val Asn Ile Thr Asn
 275 280 285
 Lys Gly Phe Ala Gly Ala Ala Asn Asn Ser Ile Asn Asn Asn Asn Gly
 290 295 300
 Leu Ala Ser Tyr Gly Gly Thr Gly Val Thr Val Ala Ala Thr Ser Pro
 305 310 315 320
 Gly Thr Ser Ser Ala Glu Asn Asn Ser Leu Ser Pro Val Pro Tyr Val
 325 330 335
 Leu Asn Arg Gly Arg Arg Ser Asn Thr Gly Leu Glu Lys Val Ile Glu
 340 345 350
 Arg Arg Gln Arg Arg Met Ile Lys Asn Arg Glu Ser Ala Ala Arg Ser
 355 360 365
 Arg Ala Arg Lys Gln Ala Tyr Thr Leu Glu Leu Glu Ala Glu Ile Glu
 370 375 380
 Lys Leu Lys Lys Thr Asn Gln Glu Leu Gln Lys Lys Gln Ala Glu Met
 385 390 395 400
 Val Glu Met Gln Lys Asn Glu Leu Lys Glu Thr Ser Lys Arg Pro Trp
 405 410 415
 Gly Ser Lys Arg Gln Cys Leu Arg Arg Thr Leu Thr Gly Pro Trp
 420 425 430
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 9
 &lt;211&gt; LENGTH: 12
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 9
 ggacacgtgg cg 12
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 10
 &lt;211&gt; LENGTH: 36
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 10
 ggacacgtgg cgggacacgt ggcgggacac gtggcg 36
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 11
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 11
 aattccggac acgtggcgta agct 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 12
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 12
 aattccggac ctacagccta agct 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 13
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 13
 aattccggac gcgtggccta agct 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 14
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 14
 aattccggac ctacagccta agct 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 15
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 15
 gaagcttgat cctcctagtt gtac 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 16
 &lt;211&gt; LENGTH: 22
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 16
 atttgaacaa gggttttagg gc 22
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 17
 &lt;211&gt; LENGTH: 24
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 17
 ttacaatcac ccacagaacc tgcc 24
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 18
 &lt;211&gt; LENGTH: 21
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 18
 gatttcgttg ccactcttaa g 21
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 19
 &lt;211&gt; LENGTH: 41
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;220&gt; FEATURE:
 &lt;221&gt; NAME/KEY: misc_feature
 &lt;222&gt; LOCATION: (1)...(41)
 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G
 &lt;400&gt; SEQUENCE: 19
 cagttgagcc gatcctgtcg nsgaggcgaa tcagtgcaac t 41
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 20
 &lt;211&gt; LENGTH: 20
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 20
 agttgcactg aattcgcctc 20
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 21
 &lt;211&gt; LENGTH: 20
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 21
 cagttgagcg gatcctgtcg 20
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 22
 &lt;211&gt; LENGTH: 10
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 22
 gacacgtgtc 10
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 23
 &lt;211&gt; LENGTH: 10
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 23
 gacacgtgtc 10
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 24
 &lt;211&gt; LENGTH: 11
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;220&gt; FEATURE:
 &lt;221&gt; NAME/KEY: misc_feature
 &lt;222&gt; LOCATION: (1)...(11)
 &lt;223&gt; OTHER INFORMATION: n = A,T,C or G
 &lt;400&gt; SEQUENCE: 24
 gntgacgtgg c 11
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 25
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 25
 Pro Val Glu Lys Val Val Glu Arg Arg Gln Arg Arg Met Ile Lys Asn
 1 5 10 15
 Arg Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Val
 20 25 30
 Glu Leu Glu Ala Glu Leu Asn Met Leu Lys Glu Glu Asn Ala Gln Leu
 35 40 45
 Lys Gln Ala Leu Ala Glu Ile Glu Arg Lys Arg Lys Gln
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 26
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 26
 Pro Met Glu Lys Thr Val Glu Arg Arg Gln Lys Arg Met Ile Lys Asn
 1 5 10 15
 Arg Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr His
 20 25 30
 Glu Leu Glu Asn Lys Val Ser Arg Leu Glu Glu Glu Asn Glu Arg Leu
 35 40 45
 Arg Arg Glu Lys Glu Val Glu Lys Val Ile Pro Trp Val
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 27
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 27
 Pro Ile Glu Lys Thr Val Glu Arg Arg Gln Lys Arg Met Ile Lys Asn
 1 5 10 15
 Arg Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr His
 20 25 30
 Glu Leu Glu Asn Lys Ile Ser Arg Leu Glu Glu Glu Asn Glu Leu Leu
 35 40 45
 Lys Arg Gln Lys Glu Val Gly Met Val Leu Pro Ser Ala
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 28
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 28
 Pro Asn Asp Thr Thr Asp Glu Arg Lys Arg Lys Arg Met Leu Ser Asn
 1 5 10 15
 Arg Glu Ser Ala Arg Arg Ser Arg Ala Arg Lys Gln Gln Arg Leu Glu
 20 25 30
 Glu Leu Val Ala Glu Val Ala Arg Leu Gln Ala Glu Asn Ala Ala Thr
 35 40 45
 Gln Ala Arg Thr Ala Ala Leu Glu Arg Asp Leu Gly Arg
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 29
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 29
 Pro Met Asp Glu Arg Glu Leu Lys Arg Glu Arg Arg Lys Gln Ser Asn
 1 5 10 15
 Arg Glu Ser Ala Arg Arg Ser Arg Leu Arg Lys Gln Gln Glu Cys Glu
 20 25 30
 Glu Leu Ala Gln Lys Val Ser Glu Leu Thr Ala Ala Asn Gly Thr Leu
 35 40 45
 Arg Ser Glu Leu Asp Gln Leu Lys Lys Asp Cys Lys Thr
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 30
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 30
 Pro Lys Asp Asp Lys Glu Ser Lys Arg Glu Arg Arg Lys Gln Ser Asn
 1 5 10 15
 Arg Glu Ser Ala Arg Arg Ser Arg Leu Arg Lys Gln Ala Glu Thr Glu
 20 25 30
 Glu Leu Ala Arg Lys Val Glu Leu Leu Thr Ala Glu Asn Thr Ser Leu
 35 40 45
 Arg Arg Glu Ile Ser Arg Leu Thr Glu Ser Ser Lys Lys
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 31
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 31
 Pro Gln Asn Glu Arg Glu Leu Lys Arg Glu Arg Arg Lys Gln Ser Asn
 1 5 10 15
 Arg Glu Ser Ala Arg Arg Ser Arg Leu Arg Lys Gln Ala Glu Thr Glu
 20 25 30
 Glu Leu Ala Arg Lys Val Glu Ala Leu Thr Ala Glu Asn Met Ala Leu
 35 40 45
 Arg Ser Glu Leu Asn Gln Leu Asn Glu Lys Ser Asp Lys
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 32
 &lt;211&gt; LENGTH: 61
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 32
 Pro Gln Asn Glu Arg Glu Leu Lys Arg Glu Lys Arg Lys Gln Ser Asn
 1 5 10 15
 Arg Glu Ser Ala Arg Arg Ser Arg Leu Arg Lys Gln Ala Glu Ala Glu
 20 25 30
 Glu Leu Ala Ile Arg Val Gln Ser Leu Thr Ala Glu Asn Met Thr Leu
 35 40 45
 Lys Ser Glu Ile Asn Lys Leu Met Glu Asn Ser Glu Lys
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 33
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 33
 ggatcctgtc gtggggacac gtggcatacg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 34
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 34
 ggatcctgtc ggggacacgt ggcgctaacg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 35
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 35
 ggatcctgtc gggacacgtg gcgcaacacg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 36
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 36
 ggatcctgtc gggacacgtg gcccacccgg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 37
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 37
 ggatcctgtc gggacacgtg gcacaaatag aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 38
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 38
 ggatcctgtc gtcaatggac acgtggctag aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 39
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 39
 ggatcctgtc gtcggacacg tggcacgaag aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 40
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 40
 gaattcgcct cgacaggaca cgtggcacgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 41
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 41
 ggatcctgtc gatcaatgga cacgtggcag aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 42
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 42
 gaattcgcct cggtgacacg tggcttgacc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 43
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 43
 ggatcctgtc ggaagtggtg acacgtggcg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 44
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 44
 gaattcgcct caagaggtga cacgtggcac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 45
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 45
 ggatcctgtc gcgacacgtg gctgttagtg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 46
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 46
 gaattcgcct ctaaggaaca cgtggcccgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 47
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 47
 gaattcgcct ccgggcggaa cacgtggcac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 48
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 48
 ggatcctgtc gcgtgggtac acgtggcccg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 49
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 49
 ggatcctgtc gcggtcttta tgacacgtgg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 50
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 50
 gaattcgcct cggacacgtg tsgcgatccc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 51
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 51
 gaattcgcct ctaaggcggg acacgtgtsc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 52
 &lt;211&gt; LENGTH: 39
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 52
 gaattcgcct ctgacactgt cagtcccacg acaggatcc 39
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 53
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 53
 gaattcgcct cggggccacg tggcttccgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 54
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 54
 gaattcgcct cttcgatggc cacgtggcgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 55
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 55
 gaattcgcct cttaagtggc cacgtggcgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 56
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 56
 gaattcgcct ctcacgaggc cacgtggcac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 57
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 57
 gaattcgcct ccgtggcgcc acgtggccgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 58
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 58
 gaattcgcct caatgcaccg ccacgtggcc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 59
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 59
 gaattcgcct ccctgactgc cacgtggcac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 60
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 60
 gaattcgcct ccaagcgttc gccacgtggc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 61
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 61
 gaattcgcct ctttgtccac gtggcccacc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 62
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 62
 gaattcgcct ctagaccgtc cacgtggccc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 63
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 63
 gaattcgcct ctaccacgtg gcacaccgtc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 64
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 64
 ggatcctgtc ggctaccacg tggcaagaag aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 65
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 65
 gaattcgcct cccttagcac cacgtggcac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 66
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 66
 ggatcctgtc ggttcgatga cgtggcgagg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 67
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 67
 ggatcctgtc ggcttgatga cgtggccacg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 68
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 68
 gaattcgcct ccttgatgac gtggcaccac gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 69
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 69
 ggatcctgtc gtggctgacg tggcactagg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 70
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 70
 ggatcctgtc ggcgcgtggt gacgtggccg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 71
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 71
 ggattctgtc gattcggtga cgtgtcccgg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 72
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 72
 gaattcgcct ctggctgctg acgtgtcccc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 73
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 73
 ggatcctgtc gacgtggcaa cttgaacgcg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 74
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 74
 gaattcgcct cgccctgaag tggacagcgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 75
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 75
 gaattcgcct cgccctgaag tggacagcgc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 76
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 76
 gaattcgcct cccgtccgcg tggcagcagc gacaggatcc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 77
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 77
 ggatcctgtc ggcgcgtggt gacgtggccg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 78
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 78
 ggatcctgtc gcgtgggtac acgtggcccg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 79
 &lt;211&gt; LENGTH: 40
 &lt;212&gt; TYPE: DNA
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 79
 ggatcctgtc gcgtgccacg tgtcctgtcg aggcgaattc 40
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 80
 &lt;211&gt; LENGTH: 60
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 80
 Leu Glu Lys Val Val Glu Arg Arg Gln Lys Arg Met Ile Lys Asn Arg
 1 5 10 15
 Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Leu Glu
 20 25 30
 Leu Glu Ala Glu Ile Glu Ser Leu Lys Leu Val Asn Gln Asp Leu Gln
 35 40 45
 Lys Lys Gln Ala Glu Ile Met Lys Thr His Asn Ser
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 81
 &lt;211&gt; LENGTH: 60
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 81
 Val Glu Lys Val Val Glu Arg Arg Gln Arg Arg Met Ile Lys Asn Arg
 1 5 10 15
 Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Val Glu
 20 25 30
 Leu Glu Ala Glu Val Ala Lys Leu Lys Glu Glu Asn Asp Glu Leu Gln
 35 40 45
 Arg Lys Gln Ala Arg Ile Met Glu Met Gln Lys Asn
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 82
 &lt;211&gt; LENGTH: 60
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 82
 Leu Glu Lys Val Ile Glu Arg Arg Gln Lys Arg Met Ile Lys Arg Arg
 1 5 10 15
 Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Met Glu
 20 25 30
 Leu Glu Ala Glu Ile Ala Gln Leu Lys Glu Leu Asn Glu Glu Leu Gln
 35 40 45
 Lys Lys Gln Val Glu Ile Met Glu Lys Gln Lys Asn
 50 55 60
 &lt;200&gt; SEQUENCE CHARACTERISTICS:
 &lt;210&gt; SEQ ID NO 83
 &lt;211&gt; LENGTH: 60
 &lt;212&gt; TYPE: PRT
 &lt;213&gt; ORGANISM: Arabidopsis thaliana
 &lt;400&gt; SEQUENCE: 83
 Leu Glu Lys Val Ile Glu Arg Arg Gln Arg Arg Met Ile Lys Asn Arg
 1 5 10 15
 Glu Ser Ala Ala Arg Ser Arg Ala Arg Lys Gln Ala Tyr Thr Leu Glu
 20 25 30
 Leu Glu Ala Glu Ile Glu Lys Leu Lys Lys Thr Asn Gln Glu Leu Gln
 35 40 45
 Lys Lys Gln Ala Glu Met Val Glu Met Gln Lys Asn
 50 55 60