bluuebunny/crossref_metadata_2025_split huggingface dataset:
Sequence of the HMR region on chromosome III of Saccharomyces cerevisiae
Authors: Sor Frédéric , Chéret Geneviève , Fabre Francis , Faye Gérard , Fukuhara Hiroshi 
Published: May 2005

AbstractA 10,095 base DNA fragment from the right arm of chormosome III of Saccharomyces cerevisiae has been sequenced and analysed. It encompasses the silent mating‐type locus HMR. Both HR Ma1 and HM Ra2 genes, as well as their flanking regulatory regions, have been identified. Three new open reading frames longer than 80 amino acid residues were found in this fragment. One of them (YCR137) shows features compatible with a membranous localization and a tansporter function. The other two do not show a similarity with any known gene. A new gene coding for tRNAthra1 (ACU) has been identified. It is located in a region coding for several delta sequences.
Development of a strain of Hansenula polymorpha for the efficient expression of guar α‐galactosidase
Authors: Veale R. A. , Giuseppin M. L. F. , Van Eijk H. M. J. , Sudbery P. E. , Verrips C. T. 
Published: May 2005

AbstractA strain of the methylotrophic yeast Hansenula polymorpha, A16 has been developed that expresses the guar α‐galactosidase gene to 22.4 mg/g dry cell weight in chemostat cultures at a dilution rate of 0.1 h−1. This corresponds to more than 13.1% of solube cell protein, of which 56–62% is secreted into the medium. The α‐galactosidase gene was flanked by the promoter and terminator sequences of the H. polymorpha mox gene, which can direct expression of the mox gene itself more than 30% of total cell protein under methanol growth. The expression cassette (pUR3510) based on the Saccharomyces cerevisiae plasmid, YEp13, was integrated into the genome. Such transformants were stable in chemostat cultures and exhibited 100% stability for both α‐galactosidase+ and leu+ phenotypes. Chemostat cultures produced higher levels of α‐galactosidase with higher specific productive expressed as mg α‐galactosidase g−1 h−1 compared to batch cultures.
Transport of malic acid in the yeast Schizosaccharomyces pombe: Evidence for proton‐dicarboxylate symport
Authors: Sousa Maria João , Mota Manuel , Leão Cecília 
Published: May 2005

AbstractThe transport system for malic acid present in Schizosaccharomyces pombe cells, growing in batch culture on several corbon sources, has been studied. It was found that the diarboxylic acid crrier of S. Pombe is a proton‐dicarboxylate symporter that allows transport and accumulation as a function of ΔpH with the following kenetic parameters at pH 5·0: Vmax = 0·01 nmol of total malic acids −1 mg (dry weight) of cells, −1and Km = 0·1mM total malica acid uptake (pH 5·0) was accompanied by desappearance of extracellular protons, the uptake rates of which followed Michaelis‐Menten kinetics as a function of the acid conscentration. The Km values, calculated as the concentrations either of anions or of undissociated acid, at various extracellular pH values, pointed to the monoanionic form as the transported species. Furthermore, accumulated free acid suffered rapid efflux after the addition of the portonophore carbonyl cyanid m‐chlorophenyl hydrazone. These results suggested that the transport system was a dicarboxylateproton symporter. Growth of cells in a medium wiht glucose (up to 14%, w/v) and malic acid (1·5%, w/v) also resulted in proton‐dicarboxylate activity, suggesting that the system, besides being constitutive, was still active at high glucose concentratons. The following dicarboxylic acids acted as competitive inhibitors of malic acid transport at pH 5·0: D‐ malic acid, succinic acid, fumaria acid oxaloacetic acid, α‐Ketoglutaric acid, maleic acid, maleic and malonic acid. In addition all of these dicarboxylic acids induced proton movements that followed Michaelis–Menten kinetics. It was concluded that the malic negatively charged form (probably the monoanionic form) was transported by a proton‐symport mechanism and that the carrier appeared to be a common ‘dicarboxylat transport sysmem’. The undissociated acid entered the cells slowly by simple diffusion.
Three yeast genes, PIR1, PIR2 and PIR3, containing internal tandem repeats, are related to each other, and PIR1 and PIR2 are required for tolerance to heat shock
Authors: Toh‐E Akio , Oguchi Tomoko , Matsui Yashushi , Yasunaga Shuichi , Nisogi Hideaki , Tanaka Kazuma 
Published: May 2005

AbstractWe isolated three highly homologous genes, PIR1, PIR2 and PIR3, collectively called the PIR genes. The remarkable feature of their putative amino acid sequence is that they contain a sequence consisting of 18–19 amino acid residues repeated tandemly seven to ten times. Genes homologous to PIR were found in Kluyveromyces lactis and Zygosaccharomyces rouxii but not in Schizosaccharomyces pombe, suggesting that a set of PIR genes plays some role in budding yeast. Bias of codon usage seen in each of the PIR translation products suggests that they are expressed abundantly. The fact that disruption of each gene is viable indicates that none of them is essential. The double disruptants, pir1 pir2, were viable under various conditions, such as higher temperature (37°C) or high salt concentration, but showed a slow‐growing phenotype on an agar slab. Furthermore, they were sensitive to heat shock. Addition of a pir3 disruption to the pir1 pir2 double disruptant brought about no phenotypic difference from the original double mutant. PIR1 and PIR3 are closely linked to each other and are on chromosome XI.
Determinants of flocculence of brewer's yeast during fermentation in wort
Authors: Straver Marika H. , Aar Paul C. V. D. , Smit Gerrit , Kijne Jan W. 
Published: May 2005

AbstractAbility of Saccharomyces cerevisiae MPY3 cells to flocculate during fermentation in wort was found to be triggered after growth limitation by oxygen shortage and to coincide with a sharp increase in cell surface hydrophobicity of the cells. Presence of oxygen in the pitching wort influenced final cell number, flocculence of the cells and cell surface hydrophobicity. Flocculation ability of cells grown in air‐depleted pitching wort was hampered, concomitant with a decrease in final cell number and in final cell surface hydrophobicity. Addition of ergosterol and Tween 80 to air‐depleted wort restored normal growth of the cells as well as flocculation ability and the increase in cell surface hydrophobicity. The same parameters increased in value after addition of ergosterol and Tween 80 to a fermentation with air‐saturated pitching wort. Hydrophobicity of a non‐flocculent mutant of S. cerevisiae strain MPY3, fermenting in air‐saturated pitching wort, did not increase at cell division arrest. These results support the hypothesis that cell surface hydrophobicity is a major determinant for yeast cells to become flocculent, and suggest that shortage of sterols and unsaturated fatty acids precedes flocculence under brewing conditions.
AFG2, an essential gene in yeast, encodes a new member of the Sec18p, Pas1p, Cdc48p, TBP‐1 family of putative ATPases
Authors: Thorsness Peter E. , White Karen H. , Ong Weoi‐Choo 
Published: May 2005

AbstractA gene from Saccharomyces cerevisiae was sequenced that encodes a protein with homology to a family of putative ATPases. These homologous proteins include the yeast cell division cycle protein Cdc48p and its mammalian homologues VCP and p97; Sec18p and its mammalian homologue NSF, proteins necessary for fusion of transport vesicles to target membranes in the secretory pathway; Pas1p, a protein necessary for peroxisome biosynthesis in yeast; Yme1p, a yeast mitochondrial protein that influences the rate of DNA escape from mitochondria; and TBP‐1, MSS1 and Sug1p, proteins that interact with transcription factors. This newly sequenced gene, named AFG2 for ATPase family gene, is located on chromosome XII 5′ to the SLP1/VPS33 open reading reading frame and encodes an essential protein of 780 amino acids that is most homologous to Cdc48p.
Analysis of PFK3—A gene involved in particulate phosphofructokinase synthesis reveals additional functions of TPS2 in Saccharomyces cerevisiae
Authors: Sur I. P. , Lobo Z. , Maitra P. K. 
Published: May 2005

AbstractThe pfk3 mutation of Saccharomyces cerevisiae causes glucose‐negativity in a pfk1 genetic background, the mutant is temperature‐sensitive for growth and homozygous diploids do not sporulate. It fails to accumulate trehalose, and has an altered glycogen accumulation profile under glucose‐starvation conditions. pfk3–6, one of the alleles of pfk3, has an altered morphology, forming long chain‐like structures at 36°C. The PFK3 gene was cloned by complementation of the mutant phenotypes. Integrative transformation demonstrated that the complementing fragment encoded the authentic PFK3 gene. The disruption of the gene does not affect viability. Like the EMS‐induced pfk3 mutant, the disruptants are temperature‐sensitive and in a pfk1 genetic background are also glucose‐negative. The PFK3 transcript is induced by heat‐shock. Partial DNA sequence shows that PFK3 is identical to TPS2 (De Virgilio et al., 1993). We demonstrate that, apart from being a structural determinant of trehalose 6‐phosphate phosphatase, PFK3 (TPS2) is required for PFKII synthesis and normal regulation of S. cerevisiae response to nutrient and thermal stresses.
Characterization of MEL genes in the genus Zygosaccharomyces
Authors: Turakainen Hilkka , Hankaanpää Marja , Korhola Matti , Aho Sirpa 
Published: May 2005

AbstractWe cloned and sequenced a Zygosaccharomyces cidri MEL gene with a view to investigating the structure and regulation of yeast MEL genes. The amino acid sequence deduced from the nucleotide sequence showed 78·6% and 78·2% similarity to Saccharomyces cerevisiae and Saccharomyces pastorianus α‐galactosidases, respectively. The expression of the MEL gene in several Zygosaccharomyces strains was induced by galactose.An electrophoretic karyotype of several Zygosaccharomyces species was obtained using contour‐clamped electric field gel electrophoresis. The minimum number of chromosomes was five for Z. cidri, six for Z. fermentati, three for Z. florentinus, and four for Z. microellipsoides. The sizes of the chromosomes were generally larger than those of S. cerevisiae, the smallest containing approximately 0·4 megabase.The MEL gene was located, using the Z. cidri MEL gene as a probe, on the largest chromosome of the Z. cidri strains. In addition, a smaller chromosome (600 kb) in Z. cidri strain CBS4575 showed hybridization to the homologous MEL probe. This chromosome was absent in Z. cidri strain CBS5666. The probe hybridized to the largest chromosome of Mel+ Z. fermentati strains but failed to hybridize to any chromosome of Mel+ Z. mrakii or Z. florentinus strains. These results suggest the existence of a polymorphic MEL gene family in the yeast Zygosaccharomyces.The sequence has been deposited in the EMBL Data Library under Accession Number L24957.
Functional expression of human poly(ADP‐ribose) polymerase in Schizosaccharomyces pombe results in mitotic delay at G1, increased mutation rate, and sensitization to radiation
Authors: Avila Matías A. , Velasco Juan A. , Smulson Mark E. , Dritschilo Anatoly , Castro Rafael , Notario Vicente 
Published: May 2005

AbstractThe activity of poly(ADP‐ribose) polymerase (PADPRP), a chromatin‐associated enzyme present in most eukaryotic cells, is stimulated by DNA strand breaks, suggesting a role for the enzyme in the cellular response to DNA damage. However, the primary function of PADPRP remains unknown. We have selected Schizosaccharomyces pombe as a simple eukaryotic system in which to study PADPRP function because this fission yeast shares with mammalian cells important cellular features possibly associated with poly‐(ADP‐ribos)ylation pathways. We investigated the existence of an endogenous yeast PADPRP by DNA and RNA hybridization to mammalian probes under low‐stringency conditions and by PADPRP activity assays. Our data indicate that fission yeasts are naturally devoid of PADPRP. We therefore isolated S. pombe strains expressing PADPRP by transformation with a human full‐length PADPRP cDNA under the control of the SV40 early promoter. The human PADPRP construct was transcribed and translated in S. pombe, generating a major transcript of the same size (3.7 kb) as that detected in mammalian cells and a 113‐kDa polypeptide, identical in size to the native human PADPRP protein. Yeast recombinant PADPRP was enzymatically active and was recognized by antibodies to human PADPRP. S. pombe cells expressing PADPRP (SPT strains) showed a stable phenotype that was characterized by: (i) cell cycle retardation as a result of a specific delay at the G1 phase, (ii) decreased cell viability in stationary cultures, (iii) enhanced rates of spontaneous and radiation‐induced ade6‐ade7 mutations, and (iv) increased sensitivity to radiation. SPT strains may prove efficient tools with which to investigate PADPRP functions in eukaryotic cells.
Sequence analysis of the right end of chromosome XV in Saccharomyces cerevisiae: An insight into the structural and functional significance of sub‐telomeric repeat sequences
Authors: Pryde Fiona E. , Huckle Tonie C. , Louis Edward J. 
Published: May 2005

AbstractApproximately 3·9 kb of DNA, centromere proximal to the previously sequenced Y′ element at the right end of chromosome XV in Saccharomyces cerevisiae strain YP1, has been sequenced. A number of the known sub‐telomeric repeat sequences were identified, including Y′, core X and STRs A, B. C and D. Several of these repeat elements contain potentially functional sequences. In addition, two other members of repeated gene families were identified. The first of these shows 61% and 60% DNA sequence identity to Enolases 1 and 2 respectively. The Enolase‐like sequence appears to be species specific, with three copies being found in all strains of S. cerevisiae studied. The location of the three copies is the same for all strains. The second repeated sequence has homology with known open reading frames on chromosomes III, V and XI. There are five or six copies of this sequence in all S. cerevisiae and S. paradoxus strains studied and three in S. bayanus strains. The analysis of this region and comparison to sub‐telomeric regions on other chromosomes gives some indication as to the potential functional and structural significance of sub‐telomeric repeat sequences. In addition, these findings are consistent with the idea that sub‐telomeric regions may be targets for unusual recombination events. The updated sequence has been deposited in the EMBL and GenBank databases under Accession Number M58718.
Genetic mapping of the α‐galactosidase MEL gene family on right and left telomeres of Saccharomyces cerevisiae
Authors: Naumov Gennadi I. , Naumova Elena S. , Louis Edward J. 
Published: May 2005

AbstractThe α‐galactosidase MEL2–MEL10 genes have been genetically mapped to right and left telomere regions of the following chromosomes of Saccharomyces cerevisiae: MEL2 at VII L, MEL3 at XVI L, MEL4 at XI L, MEL5 at IV L, MEL6 at XIII R, MEL7 at VI R, MEL8 at XV R, MEL9 at X R and MEL10 at XII R. A set of tester strains with URA3 inserted into individual telomeres and no MEL genes was used for mapping.
Localization of the dominant flocculation genes FLO5 and FLO8 of Saccharomyces cerevisiae
Authors: Teunissen Aloys W. R. H. , Van Den Berg Johan A. , Steensma H. Yde 
Published: May 2005

AbstractIn the yeast Saccharomyces cerevisiae three dominant flocculation genes, FLO1, FLO5 and FLO8 have been described. Until now only the FLO1 gene, which is located at chromosome I, has been cloned and sequenced. FLO5 and FLO8 were previously localized at chromosomes I and VIII respectively (Vezinhet, F., Blondin, B. and Barre, P. (1991). Mapping of the FLO5 gene of Saccharomyces cerevisiae by transfer of a chromosome during cytoduction. Biotechnol. Lett. 13, 47–52; Yamashita, I. and Fukui, S. (1983). Mating signals control expression of both starch fermentation genes and a novel flocculation gene FLO8 in the yeast Saccharomyces. Agric. Biol. Chem. 47, 2889–2896). This was not in agreement with our results. Here, we report the location of FLO5 and FLO8 on chromosomes VIII and I respectively.By induced chromosome loss and genetic mapping, the FLO5 gene was localized at the right end of chromosome VIII approximately 34 cM centromere distal of PET3. This is part of the region that is present both at chromosome I and chromosome VIII. The location of FLO5 in this area of chromosome VIII made it necessary to re‐evaluate the localization of FLO8, which was previously thought to occur in this region. Both genetic and physical mapping showed that FLO8 is allelic to FLO1. Hence, there are only two known dominant flocculation genes, FLO1 and FLO5.Analysis of the nucleotide sequence of chromosome VIII of a non‐flocculent strain revealed an open reading frame encoding a putative protein that is approximately 96% identical to the Flo1 protein.This suggests that both dominant flocculation genes encode similar, cell wall‐associated, proteins with the same function in the flocculation mechanism.
Genetically‐modified brewing yeasts for the 21st century. Progress to date
Authors: Hammond John R. M. 
Published: May 2005

AbstractAcademic studies and traditional breeding of yeasts depend upon their sporulation lifestyle. The strains used have been specially selected to sporulate readily and to mate producing new yeast types. Unfortunately brewing yeast strains do not behave in this way. They sporulate poorly, any spores which are formed are usually non‐viable and any haploid strains produced are invariably non‐maters. Only in recent years, with the development of recombinant‐DNA techniques, has the specific breeding of new brewing yeast strains become widespread. Strains have been produced with the ability to ferment a wider range of carbohydrates, with altered flocculation properties and which produce beers with modified flavours. Many have been tested on the pilot scale and one, an amylolytic brewing yeast, has received approval for commercial use.
A Bicapped α‐Keggin Unit‐Supported Transition Metal Complex: Hydrothermal Synthesis and Characterization of [Cu(en)2(H2O)]2[Cu(en)2]0.5[Mo8V7O42{Cu(en)2}]
Authors: Zeng Qing‐Xin , Xu Ji‐Qing , Song Yu‐Jiang , Cui Xiao‐Bing , Shi Zhan 
Published: May 2005

AbstractA new metal‐oxo cluster supported transition metal complex, [Cu(en)2(H2O)]2[Cu(en)2]0.5[MoVI8VIV6VVO42{Cu(en)2}], has been synthesized under hydrothermal conditions. Its structure was determined by single‐crystal X‐ray diffraction. The compound crystallizes in the triclinic system, space group $P{\bar 1}$ (No. 2), a = 12.245(5), b = 12.669(5), c = 20.949(8) Å, α = 77.120(13), β = 78.107(17), γ = 65.560(14)°, V = 2860(2) Å3, Z = 2. The metal‐oxo cluster contains a novel bicapped a‐Keggin structure unit and a [Cu(en)2]2+ unit covalently bonded to the [Mo8V7O42]7− cluster.
{[Zn2(Bim)3(OH)(H2O)]·(DMF)(H2O)3}∞: A Two Dimensional Coordination Polymer with Layer Silicate‐like Structure
Authors: Xu Hai‐Jun , Liu You‐Xun , Shen Zhen , Tian Yun‐Qi , You Xiao‐Zeng 
Published: May 2005

AbstractA layer silicate‐like zinc(II) benzimidazolate polymer {[Zn2(Bim)3(OH)(H2O)]·(DMF)(H2O)3}∞ (1) was synthesized at room temperature and characterized with X‐ray single‐crystallography: Monoclinic, space group C2/m (No.12), a = 10.423(3) Å, b = 17.416(6) Å, c = 16.583(5) Å, β = 92.698(4), V = 3006.8(17) Å3.
Complexes of 1,3‐Bis(diphenylphosphano)propane (dppp) with Dichloroplatinum(II) and Bis(chlorogold(I)): Intramolecular versus Intermolecular AuI–AuI Association of [(μ‐dppp)(AuCl)2] in catena and cyclo Forms
Authors: Kaim Wolfgang , Dogan Akbey , Klein Axel , Záliš Stanislav 
Published: May 2005

AbstractThe compound [(μ‐dppp)(AuCl)2], previously reported to associate intermolecularly in a chain (catena) structure through AuI–AuI interactions (3.316Å), was obtained from gold(III) precursors in a cyclo form with shortened intramolecular AuI—AuI contacts at 3.237Å and a puckered AuPCCCPAu seven‐membered ring. DFT calculations using a large relativistic basis to account for the d10–d10 interaction reproduce the observed molecular structure in the crystal of this “linkage isomer”, including the conspicuous distortion at one of the gold atoms. The chelate complex [(dppp)PtCl2] was crystallized and structurally characterized as the dichloromethane solvate.
Crystal Structure of Octaethyloxyphthalocyaninato Copper, the Overlap Affect on the Ring Skeleton Distortion
Authors: Lin Mei‐Jin , Wang Jun‐Dong , Chen Nai‐Sheng 
Published: May 2005

AbstractThe crystal structure of 1,4,8,11,15,18,22,25‐octaethyloxyphthalocyaninatocopper was determined by X‐ray diffraction. The ring skeleton distortion is shown, which not only attributed to inter‐molecular steric congestion of substituents but also to the less overlap of the skeletons.
Synthesis, Crystal Structure and Luminescence of [Ag(PPh3)2(H2TMT)]
Authors: Wei Yong‐Qin , Wu Ke‐Chen , Zhuang Bo‐Tao , Zhou Zhang‐Feng , Zhang Ming‐Xin , Liu Cai‐Ping 
Published: May 2005

AbstractThe silver complex Ag(PPh3)2(H2TMT) (1)(H3TMT = 2,4,6‐trimercapto‐1,3,5‐triazine) has been synthesized and characterized. The ligand trimercaptotriazine exhibits a novel coordination mode and the complex shows a special hydrogen bonding linkage in the crystal packing. The colorless crystals of 1 exhibit broad emission in the visible region at room temperature. TDDFT calculation indicated that the π–π attraction is crucial for fluorescence of the title complex.
Kristallstruktur und Schwingungsspektrum von (H2NPPh3)2[SnCl6]·2CH3CN
Authors: Neumüller Bernhard , Weller Frank , Dehnicke Kurt 
Published: May 2005

AbstractCrystal Structure and Vibrational Spectrum of (H2NPPh3)2[SnCl6]·2CH3CNSingle crystals of (H2NPPh3)2[SnCl6]·2CH3CN (1) were obtained by oxidative addition of tin(II) chloride with N‐chloro‐triphenylphosphanimine in acetonitrile in the presence of water. 1 is characterized by IR and Raman spectroscopy as well as by a single crystal structure determination: Space group ${\rm P}{\bar 1}$, Z = 2, lattice dimensions at 193 K: a = 1029.6(1), b = 1441.0(2), c = 1446.1(2) pm, α = 90.91(1)°, β = 92.21(1)°, γ = 92.98(1)°, R1 = 0.0332. 1 forms an ionic structure with two different site positions of the [SnCl6]2− ions. One of them is surrounded by four N‐hydrogen atoms of four (H2NPPh3)+ ions, four CH3CN molecules form N–H···N≡C–CH3 contacts with the other four N‐hydrogen atoms of the cations. Thus, 1 can be written as [(H2NPPh3)4(CH3CN)4(SnCl6)]2+[SnCl6]2−.
Synthese, Kristallstruktur und Eigenschaften von Chrom(III)‐trimetaphosphimat‐Heptahydrat, Cr(PO2NH)3·7H2O
Authors: Correll Sascha , Sedlmaier Stefan , Schnick Wolfgang 
Published: May 2005

AbstractSynthesis, Crystal Structure, and Properties of Chromium(III) Trimetaphosphimate Heptahydrate, Cr(PO2NH)3·7H2OChromium(III) trimetaphosphimate heptahydrate, Cr(PO2NH)3·7H2O, was synthesized by combining equimolar aqueous solutions of Na3(PO2NH)3·4H2O and Cr(NO3)3·9H2O. Suitable single crystals for X‐ray crystal structure determination were obtained by the reaction of an aqueous solution of Na3(PO2NH)3·4H2O with Cr(NO3)3·9H2O (molar ratio 2 : 1) using gel crystallization in gelatine gels. The structure of Cr(PO2NH)3·7H2O was solved by single‐crystal X‐ray methods (P21/n; a = 946.1(2), b = 1076.0(2), c = 1295.4(3) pm, β = 92.68(3)°; Z = 4). The P3N3 rings of the trimetaphosphimate ions exhibit a composition of the boat and the twist conformation in the ratio 1 : 1. The conformation of the anions has been analysed using torsion angles, displacement asymmetry parameters, and puckering parameters. Cr3+ is coordinated nearly octahedrally by six crystal water molecules. The trimetaphosphimate ions do not take part in that coordination. In the crystal these complex ions are interconnected by N–H···O und O–H···O hydrogen bonds. Thus, a three‐dimensional network is formed. The arrangement of the [Cr(OH2)6]3+ octahedra and the (PO2NH)33− ions can be described as a distorted variant of the CsCl structure type.