bluuebunny/crossref_metadata_2025_split huggingface dataset:
Galactose inhibition of the constitutive transport of hexoses in Saccharomyces cerevisiae
Authors: Nevado Julian , Navarro Ma Asuncion , Heredia Claudio F. 
Published: May 2005

AbstractThe relationship between the pathways of glucose and galactose utilization in Saccharomyces cerevisiae has been studied. Galactose (which is transported and phosphorylated by inducible systems) is a strong inhibitor of the utilization of glucose, fructose and mannose (which have the same constitutive transport and phosphorylation systems). Conversely, all these three hexoses inhibit the utilization of galactose, though with poor efficiency. These cross‐inhibitions only occur in yeast adapted to galactose or in galactose‐constitutive mutants.The efficiency of galactose as inhibitor is even greater than the efficiencies of each of the other three hexoses to inhibit the utilization of each other. Phosphorylation is not involved in the inhibition and the transport of sugars is the affected step.The cross‐inhibitions between galactose and either glucose, fructose or mannose do not implicate utilization of one hexose at the expense of the other, as it occurs in the mutual interactions between the latter three sugars. It seems that, by growing the yeast in galactose, a protein component is synthesized, or alternatively modified, that once bound to either galactose or any one of the other three hexoses (glucose, fructose or mannose), cross‐interacts respectively with the constitutive or the inducible transport systems, impairing their function.
Change in transport activities of vacuoles of the yeast Yarrowia lipolytica during its growth on glucose
Authors: Kulakovskaya T. V. , Matyashova R. N. , Shishkanova N. V. , Finogenova T. V. , Okorokov L. A. 
Published: May 2005

AbstractVacuoles were isolated from Yarrowia lipolytica yeast cells taken at various growth phases under carbon or nitrogen limitation. Vacuoles from the cells at the logarithmic growth phase showed a high activity of vacuolar H+‐ATPase (0·9–1·1 U/mg protein) and efficiently generated chemical proton gradient and membrane potential across the tonoplast. Ca2+‐ and citrate transport were found to be maximal at this growth phase. At growth retardation and then in the stationary phase all the parameters studied decreased irrespective of the method of growth limitation. The citrate‐transporting activity of vacuoles completely disappeared at growth retardation, also irrespective of the limitation method and irrespective of whether yeast cells overproduced citrate in the culture medium. The citrate‐transporting system of Y. lipolytica vacuolar membrane is concluded not to be involved in citrate efflux and this efflux is probably performed by the plasmalemma transport system.
Purification and characterization of highly active and stable polyphosphatase from Saccharomyces cerevisiae cell envelope
Authors: Andreeva Nadezhda A. , Okorokov Lev A. 
Published: May 2005

AbstractSaccharomyces cerevisiae cell envelope polyphosphatase was isolated in highly active and stable form by extraction from cells with zwittergent TM‐314 followed by chromatography of the extract on phosphocellulose and QAE‐Sephadex in the presence of 5 mM‐MgCl2, 0·5 mM‐EDTA and 0·1% Triton X‐100. The enzyme possessed a specific activity of 220 U/mg and after 30 days retained 87% of its activity at −20°C. Polyphosphatase molecular mass was determined to be about 40 kDa by gel filtration and polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate. The enzyme hydrolysed polyphosphates with various chain lengths (n = 3–208), had low activity for GTP and did not split pyrophosphate, ATP and p‐nitrophenylphosphate. On polyphosphates with chain lengths n = 3, 9 and 208, Km values were 1·7 × 10−4, 1·5 × 10−5 and 8·8 × 10−7 M respectively. Polyphosphatase was most active and stable at pH 6·0–8·0. The enzyme showed maximal activity at 50°C. The time of half inactivation of polyphosphatase at 40, 45 and 50°C was 45, 10 and 3 min, respectively. In the absence of divalent cations and also with Ca2+ or Cu2+, the enzyme showed practically no activity. The ability of divalent cations to activate polyphosphatase was reduced in the following order: Co2+ > Mg2+ > Mn2+ > Fe2+ > Zn2+. Polyphosphatase was completely inhibited by 1 mM‐ammonium molybdate and 50 μM‐Zn2+ or Cu2+ (in the presence of Mg2+).
Cystathionine γ‐lyase of Saccharomyces cerevisiae: Structural gene and cystathionine γ‐synthase activity
Authors: Ono Bun‐Ichiro , Ishii Nobuya , Naito Kazuhide , Miyoshi Shin‐Ichi , Shinoda Sumio , Yamamoto Sumiyo , Ohmori Shinji 
Published: May 2005

AbstractPurification of Saccharomyces cerevisiae cystathionine γ‐lyase (γ‐CTLase) was hampered by the presence of a protein migrating very close to it in various types of column chromatography. The enzyme and the contaminant were nevertheless separated by polyacrylamide gel electrophoresis. N‐terminal amino acid sequence analysis indicated that they are coded for by CYS3(CYI1) and MET17(MET25), respectively, leading to the conclusion that CYS3 is the structural gene for γ‐CTLase and that the contaminant is O‐acetylserine/O‐acetylhomoserine sulfhydrylase (OAS/OAH SHLase). Based on these findings, we purified γ‐CTLase by the following strategy: (1) extraction of OAS/OAH SHLase from a CYS3‐disrupted strain; (2) preparation of antiserum against it; (3) identification of a strain devoid of the OAS/OAH SHLase protein using this antiserum; and (4) extraction of γ‐CTLase from this strain. Purified γ‐CTLase had cystathionine γ‐synthase (γ‐CTSase) activity if O‐succinylhomoserine, but not O‐acetylhomoserine, was used as substrate. From this notion we discuss the evolutional relationship between S. cerevisiae γ‐CTLase and Escherichia coli γ‐CTSase.
Genetics of heat‐curability of killer virus of yeast
Authors: Weinstein Lee Ann , Capaldo‐Kimball Florence , Leibowitz Michael J. 
Published: May 2005

AbstractThe cytoplasmically inherited M double‐stranded (ds) RNA genome segment of killer virus of Saccharomyces cerevisiae is heat‐curable in some yeast strains but not in others. Temperature sensitivity is conferred on both M1 and M2 dsRNA satellite virus segments by the L‐A‐HN allele of the killer helper virus genome, but not by the L‐A‐H allele. Both diploidy and mating type heterozygosity of the host cell are also correlated with increased virus curability.
Genetic and physical localization of the acetyl‐coenzyme A synthetase gene ACS1 on chromosome I of Saccharomyces cerevisiae
Authors: Steensma H. Yde , Barth Gerold , De Virgilio Claudio 
Published: May 2005

AbstractThe ACS1 gene, encoding acetyl‐coenzyme A synthetase, was mapped genetically at the left arm of chromosome I between pURA3 and PYK1 at 19 and 28 cM respectively. Comparison with the physical map defined a recombinational ‘hot‐spot’ in this region in addition to the one between CDC24 and PYK1.
Genes required for derepression of an extracellular glucoamylase gene, STA2, in the yeast Saccharomyces
Authors: Kuchin S. V. , Kartasheva N. N. , Benevolensky S. V. 
Published: May 2005

AbstractA diastatic strain of Saccharomyces cerevisiae producing the STA2‐encoded extracellular glucoamylase (GA) in a pronounced glucose‐repressible fashion was used as a parent for generating mutants with reduced GA activity under normal conditions of derepression. In addition to mutations in STA2, five other recessive mutations were identified which fell into four complementation groups designated haf1 through haf4. RNA blot analysis suggested that the haf mutations confer defects in STA2 transcription. The haf mutants were pleiotropically defective in utilization of alternative carbon sources and resembled the snf (sucrose non‐fermenting) mutants identified previously as unable to derepress the expression of the SUC2 gene encoding invertase. We present evidence strongly suggesting that haf1 = snf2, haf3 = snf1 and haf4 = snf5. By phenotypic criteria, the postulated HAF2 gene (which is none of the SNF genes tested) appears to be similar to SNF2, SNF5 and SNF6, and is possibly a non‐redundant extension of this group of functionally related SNF genes.
Para‐aminobenzoate synthase gene of Saccharomyces cerevisiae encodes a bifunctional enzyme
Authors: Edman Jeffrey C. , Goldstein Alan L. , Erbe Jennifer G. 
Published: May 2005

AbstractThe Saccharomyces cerevisiae gene for para‐aminobenzoate (PABA) synthase has been identified based upon its ability to confer sulfonamide resistance when present on a multicopy episomal vector. The 3840 bp DNA sequence fragment reported here contains a 2199 bp open reading frame encoding a 733 amino acid protein with similarity to the two components of PABA synthase described for prokaryotes (Escherichia coli PabA and PabB), suggesting that PABA synthase is bifunctional in yeast. The cloned sequence was confirmed to be PABA synthase by gene disruption. Chromosome gel analysis places the gene for PABA synthase on chromosome XIV.
Molecular characterization of the SEC1 gene of Saccharomyces cerevisiae: Subcellular distribution of a protein required for yeast protein secretion
Authors: Egerton Mark , Zueco Jesus , Boyd Alan 
Published: May 2005

AbstractStrains of Saccharomyces cerevisiae harbouring temperature‐sensitive mutations in the SEC1 and SEC5 genes exhibit an accumulation of post‐Golgi secretory vesicles at 37°C. We have cloned a fragment of yeast DNA which carries two distinct genes, one of which complements a sec1 mutation, and the other a sec5 mutation. Genetic tests confirm that the sec1‐complementing gene is indeed SEC1, and is essential for cell growth. Nucleotide sequence analysis reveals that the cloned SEC1 gene is the same as a previously sequenced sec1‐complementing gene. The SEC1 sequence encodes a protein of 724 amino acids with a predicted molecular mass of 83 kDa. Antibodies purified from a polyclonal antiserum raised against the protein product of the cloned gene recognize a yeast protein of apparent molecular mass 78 kDa which is found in a detergent‐resistant association with a rapidly sedimenting yeast subcellular fraction, behaviour which is suggestive of an interaction with a component of the yeast cytoskeleton.
Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine‐specific permease
Authors: Sychrova H. , Chevallier M. R. 
Published: May 2005

AbstractThe LYP1 gene of Saccharomyces cerevisiae was cloned by complementation in lysine‐permease‐deficint recipient yeast cells, and its nucleotide sequence was determined. An open reading frame of 1833 nucleotides was found encoding a polypeptide of 611 amino acids, with a calculated molecular weight of 68 118. Analysis of the deduced primary structure of the protein revealed ten membrane‐spanning regions and three potential N‐glycosylation sites. Analysis of the deduced sequence of protein LYP1 indicates homology with other yeast amino‐acid permeases, in particular with CAN1, and also the lysine‐specific permease of Escherichia coli. The strain transformed by a multi‐copy plasmid harbouring the LYP1 gene, showed a 20‐fold increase in the maximum velocity of lysine uptake over that in the wild type, with no changes in the affinity of the permease for its substrate.
Flocculation of Kluyveromyces marxianus is induced by a temperature upshift
Authors: Fernandes P. A. , Moradas‐Ferreira P. , Sousa M. 
Published: May 2005

AbstractAn upshift of the growth temperature from 26 to 40°C in the presence of calcium leads to the aggregation of Kluyveromyces marxianus cells and to the formation of flocs. Analysis of cell wall proteins, either by sodium dodecyl sulphate–polyacrylamide gel electrophoresis of extractable mannoproteins or by immunolocalization, revealed an accumulation of a protein with Mr 37 kDa (p37), upon flocculation. Immunological studies confirmed the homology of this protein with the glycolytic enzyme glyceraldehyde‐3‐phosphate dehydrogenase (GAPDH). When mRNA isolated from cells growing at 40°C was translated in vitro, a 35 kDa newly labelled protein was synthesized and immunoprecipitation assays showed that this protein is recognized by p37‐antiserum, suggesting that the 35 kDa polypeptide might be an unglycosylated precursor form of p37. The results indicated that the presence of this cell wall mannoprotein closely related to GAPDH is dependent on the growth temperature, suggesting its role as adhesin.
Metabolic studies of a fructose‐intolerant yeast by in vivo31P‐nuclear magnetic resonance spectroscopy
Authors: Doyle Timothy C. , Donaldson Iain A. , Spickett Corinne M. , Ratcliffe R. George 
Published: May 2005

AbstractThe metabolic effects of the administration of fructose to a yeast expressing the cDNA for rat liver ketohexokinase have been investigated by 31P‐nuclear magnetic resonance spectroscopy. Cessation of growth suffered by the yeast on exposure to 5 and 25 mM‐fructose was accompanied by a large accumulation of fructose 1‐phosphate at the expense of cytoplasmic orthophosphate and nucleoside triphosphate. Shifts in resonances were consistent with a drop in cytoplasmic pH. Arresting growth with 1 mM‐fructose, however, did not result in these changes, although a large accumulation of fructose 1‐phosphate occurred which may have been supported by the mobilization of polyphosphates.
Identification of two divergently transcribed genes centromere‐proximal to the ARG4 locus on chromosome VIII of Saccharomyces cerevisiae
Authors: Rocco Vincenzo , Daly Michael J. , Matre Vilborg , Lichten Michael , Nicolas Alain 
Published: May 2005

AbstractWe have sequenced a 3296 bp segment of the chromosome VIII adjacent to the 3′ end of the ARG4 gene. This segment contains two divergently oriented open reading frames (YSC83 and YSC84). Northern blot analysis showed the presence of transcripts corresponding to these two open reading frames in vegetative cells. Levels of these transcripts increase five to ten‐fold during sporulation. These two genes are not essential for vegetative growth or sporulation. Analysis of the putative protein products on the SwissProt database revealed that the C‐terminal region of the Ysc84 protein contains a putative SH3 domain.
A comparative analysis of distinctive features of yeast protein sequences
Authors: Sapolsky Ronald J. , Brendel Volker , Karlin Samuel 
Published: May 2005

AbstractThe recently published sequence of yeast chromosome III (YCIII) provides the longest continuous stretch of a eukaryotic DNA molecule sequenced to date (315 kb). The sequence contains 116 distinct AUG‐initiated open reading frames of at least 200 codons in length, more than 50 of which had not been described previously nor bear significant similarity to known proteins. We have analysed the YCIII known and putative‐protein sequences with respect to significant statistical features which might reflect on structural and functional characteristics. The YCIII proteins have striking similarities and differences in their sequence attribute distributions compared to the corresponding distributions for all available yeast sequences and other protein collections. Nine examples of YCIII proteins with distinctive sequence features are discussed in detail.
Accurate initiation of mRNA synthesis in extracts from Schizosaccharomyces pombe, kluyveromyces lactis and Candida glabrata
Authors: Woontner Michael , Jaehning Judith A. 
Published: May 2005

AbstractWe demonstrate the successful adaptation to other yeast species of a protocol previously described for production of transcriptionally active whole cell extracts from Saccharomyces cerevisiae (Woontner and Jaehning, 1990, J. Biol. Chem. 265, 8979–8982). Extracts prepared from Schizosaccharomyces pombe, Kluyveromyces lactis and Candida glabrata were all capable of initiating transcription from a template containing the S. cerevisiae CYC1 TATA box fused to a G‐less cassette. Transcription in all of the extracts was sensitive to inhibition by α‐amanitin, indicating that it was catalysed by RNA polymerase II, and was dramatically stimulated by the chimeric activator GAL4/VP16. The different extracts used different subsets of a group of three initiation sites.
The complete sequence of a 15 820 bp segment of Saccharomyces cerevisiae chromosome XI contains the UBI2 and MPL1 genes and three new open reading frames
Authors: Bou German , Esteban Pedro F. , Baladron Victoriano , Gonzalez Gloria A. , Cantalejo Jesus Garcia , Remacha Miguel , Jimenez Antonio , Del Rey Francisco , Ballesta Juan P. G. , Revuelta José L. 
Published: May 2005

AbstractAs part of the EEC yeast genome program, a fragment of 15 820 bp from the right arm of Saccharomyces cerevisiae chromosome XI has been sequenced. This fragment corresponds roughly to the centromere‐distal half of cosmid pUKG046 and to a small fragment of cosmid pUKG096, which are located approximately 150 kb from the centromere. It contains four open reading frames (ORFs) which encode potential proteins of more than 100 amino acid residues, as well as the UBI2 gene which carries an intron and does not show up as an ORF in the sequence analysis programs. One of the putative proteins, YKR412, is very rich in serine and has significant homology at the carboxyl end to Nopp140 phosphoprotein. YKR413 has several predicted transmembrane domains. YKR15, which has been recently cloned as the MPL1 gene, encodes a polypeptide that shows homologies to myosin heavy chain and to the cytoskeleton protein Uso1.
Inhibition of protein synthesis disrupts the golgi apparatus in the fission yeast, Schizosaccharomyces pombe
Authors: Ayscough Kathryn , Warren Graham 
Published: May 2005

AbstractSchizosaccharomyces pombe was treated with either cycloheximide or anisomycin at levels sufficient to inhibit >95% of protein synthesis for periods upon to 3 h, equivalent to one cell cycle. Treatment for as little as 1 h caused significant loss of the Golgi apparatus by both immunofluorescence and electron microscopy. The loss was quantitated by stereology on electron micrographs. Nearly 90% of the stacked Golgi was lost over a 3 h period. No other intracellular membrane compartment seemed to be affected. Measurement of enzyme activities confirmed these observations. The activity of a resident of the Golgi apparatus, α‐1,2 galactosyltransferase, was reduced over this time, whereas the endoplasmic reticulum marker, BiP, and the cytoplasmic enzyme, hexokinase, were unaffected. The morphological changes associated with cycloheximide addition were reversed on its removal, though there was a lag before cells recommenced growth or secretion of the enzyme, acid phosphatase.
A physical comparison of chromosome III in six strains of Saccharomyces cerevisiae
Authors: Wicksteed Barton L. , Collins Irene , Dershowitz Ann , Stateva Lubomira I. , Green Rebecca P. , Oliver Stephen G. , Brown Alistair J. P. , Newlon Carol S. 
Published: May 2005

AbstractWe have tested the clones used in the European Yeast Chromosome III Sequencing Programme for possible artefacts that might have been introduced during cloning or passage through Escherichia coli. Southern analysis was performed to compare the BamHI, EcoRI, HindIII and PstI restriction pattern for each clone with that of the corresponding locus on chromosome III in the parental yeast strain. In addition, further enzymes were used to compare the restriction maps of most clones with the map predicted by the nucleotide sequence (Oliver et al., 1992). Only four of 506 6‐bp restriction sites predicted by the sequence were not observed experimentally. No significant cloning artefacts appear to disrupt the published sequence of chromosome III. The restriction patterns of six yeast strains have also been compared. In addition to two previously identified sites of Ty integration on chromosome III (Warmington et al., 1986; Stucka et al., 1989; Newlon et al., 1991), a new polymorphic site involving Ty retrotransposition (the Far Right‐Arm transposition Hot‐Spot, FRAHS) has been identified close to CRY1. On the basis of simple restriction polymorphisms, the strains S288C, AB972 and W303‐1b are closely related, while XJ24‐24a and J178 are more distant relatives of S288C. A polyploid distillery yeast is heterozygous for many polymorphisms, particularly on the right arm of the chromosome.
Molecular characterization of the SPT23 gene: A dosage‐dependent suppressor of ty‐induced promoter mutations from Saccharomyces cerevisiae
Authors: Burkett Thomas J. , Garfinkel David J. 
Published: May 2005

AbstractSPT genes are suppressors of mutations induced by the retrotransposon Ty in Saccharomyces cerevisiae. All SPT genes isolated to date suppress Ty‐induced mutations by altering transcription. SPT23 was identified as a multicopy suppressor of the Ty‐induced promoter mutations his4‐912δ and lys2‐61. Multicopy expression of SPT23 suppresses a variety of Ty‐induced promoter mutations, including the MAT‐regulated alleles his4‐917 (480) and lys2‐173R2. Here, we report the initial characterization of the SPT23 gene, including its nucleotide sequence and location in the yeast genome. The SPT23 gene contains a 1854 base pair open reading frame. Searches of the current data bases show no homology between SPT23 and previously described genes or proteins. The SPT23 gene is located between RAM2 and MAK11 on the left arm of chromosome XI. Tn10‐LUK insertional mutagenesis of the SPT23 gene indicates that SPT23 is not essential for vegetative growth and spt23 mutations do not confer an Spt− phenotype.
Erratum to: Sequence of a 4.8 kb fragment of Saccharomyces cerevisiae chromosome II including three essential open reading frames
Authors: Baur Axel , Schaaff‐Gerstenschläger Ine , Boles Eckhard , Miosga Thomas , Rose Matthias , Zimmermann Friedrich K. 
Published: May 2005

AbstractThe above paper (Yeast 9:, 289–293, 1993) erroneously presented a non‐updated sequence due to data‐transmission errors. The corrected sequence is 4939 bp in length and has been deposited in the EMBL Data Library under the accession number X71329. Consequently the amino acid sequences of YBR 12.03 and YBR 12.05 changed.
VI. Yeast sequencing reports. The sequence and potential regulatory elements of the HEM2 promoter of Saccharomyces cerevisiae
Authors: Schlaepfer Isabel R. , Mattoon James R. , Bajszár George 
Published: May 2005

AbstractThis paper reports the 1890‐bp sequence located upstream of the HEM2 gene of Saccharomyces cerevisiae. The following potential regulatory protein‐binding motifs were found: ABF1‐binding site, yAP1‐binding site, two REB1‐binding sites, a cyclic AMP‐responsive element, RAP1‐binding site, and several HAP2‐HAP3‐HAP4 binding sites, implicating a complex regulatory mechanism governing expression for the HEM2 gene.