Two functional alpha-tubulin genes of the yeast Saccharomyces cerevisiae encode divergent proteins.

Two alpha-tubulin genes from the budding yeast Saccharomyces cerevisiae were identified and cloned by cross-species DNA homology. Nucleotide sequencing studies revealed that the two genes, named TUB1 and TUB3, encoded gene products of 447 and 445 amino acids, respectively, that are highly homologous to alpha-tubulins from other species. Comparison of the sequences of the two genes revealed a 19% divergence between the nucleotide sequences and a 10% divergence between the amino acid sequences. Each gene had a single intervening sequence, located at an identical position in codon 9. Cell fractionation studies showed that both gene products were present in yeast microtubules. These two genes, along with the TUB2 beta-tubulin gene, probably encode the entire complement of tubulin in budding yeast cells.

Download Full-text

GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats

Molecular and Cellular Biology ◽

10.1128/mcb.11.10.5101-5112.1991 ◽

1991 ◽

Vol 11 (10) ◽

pp. 5101-5112

Author(s):

J S Flick ◽

M Johnston

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Interactions ◽

Tandem Repeats ◽

Glucose Repression ◽

Molecular Data ◽

Primary Response ◽

Yeast Cells ◽

Cell Fractionation ◽

Protein Protein Interactions ◽

Yeast Saccharomyces Cerevisiae

Growth of the yeast Saccharomyces cerevisiae on glucose leads to repression of transcription of many genes required for alternative carbohydrate metabolism. The GRR1 gene appears to be of central importance to the glucose repression mechanism, because mutations in GRR1 result in a pleiotropic loss of glucose repression (R. Bailey and A. Woodword, Mol. Gen. Genet. 193:507-512, 1984). We have isolated the GRR1 gene and determined that null mutants are viable and display a number of growth defects in addition to the loss of glucose repression. Surprisingly, grr1 mutations convert SUC2, normally a glucose-repressed gene, into a glucose-induced gene. GRR1 encodes a protein of 1,151 amino acids that is expressed constitutively at low levels in yeast cells. GRR1 protein contains 12 tandem repeats of a sequence similar to leucine-rich motifs found in other proteins that may mediate protein-protein interactions. Indeed, cell fractionation studies are consistent with this view, suggesting that GRR1 protein is tightly associated with a particulate protein fraction in yeast extracts. The combined genetic and molecular data are consistent with the idea that GRR1 protein is a primary response element in the glucose repression pathway and is required for the generation or interpretation of the signal that induces glucose repression.

Download Full-text

Either of the major H2A genes but not an evolutionarily conserved H2A.F/Z variant of Tetrahymena thermophila can function as the sole H2A gene in the yeast Saccharomyces cerevisiae.

Molecular and Cellular Biology ◽

10.1128/mcb.16.6.2878 ◽

1996 ◽

Vol 16 (6) ◽

pp. 2878-2887 ◽

Cited By ~ 11

Author(s):

X Liu ◽

J Bowen ◽

M A Gorovsky

Keyword(s):

Saccharomyces Cerevisiae ◽

Tetrahymena Thermophila ◽

Yeast Species ◽

Budding Yeast ◽

Yeast Cells ◽

Ciliated Protozoan ◽

Yeast Saccharomyces Cerevisiae ◽

Evolutionarily Conserved ◽

Cold Sensitive ◽

Conserved Epitope

H2A.F/Z histones are conserved variants that diverged from major H2A proteins early in evolution, suggesting they perform an important function distinct from major H2A proteins. Antisera specific for hv1, the H2A.F/Z variant of the ciliated protozoan Tetrahymena thermophila, cross-react with proteins from Saccharomyces cerevisiae. However, no H2A.F/Z variant has been reported in this budding yeast species. We sought to distinguish among three explanations for these observations: (i) that S. cerevisiae has an undiscovered H2A.F/Z variant, (ii) that the major S. cerevisiae H2A proteins are functionally equivalent to H2A.F/Z variants, or (iii) that the conserved epitope is found on a non-H2A molecule. Repeated attempts to clone an S. cerevisiae hv1 homolog only resulted in the cloning of the known H2A genes yHTA1 and yHTA2. To test for functional relatedness, we attempted to rescue strains lacking the yeast H2A genes with either the Tetrahymena major H2A genes (tHTA1 or tHTA2) or the gene (tHTA3) encoding hv1. Although they differ considerably in sequence from the yeast H2A genes, the major Tetrahymena H2A genes can provide the essential functions of H2A in yeast cells, the first such case of trans-species complementation of histone function. The Tetrahymena H2A genes confer a cold-sensitive phenotype. Although expressed at high levels and transported to the nucleus, hv1 cannot replace yeast H2A proteins. Proteins from S. cerevisiae strains lacking yeast H2A genes fail to cross-react with anti-hv1 antibodies. These studies make it likely that S. cerevisiae differs from most other eukaryotes in that it does not have an H2A.F/Z homolog. A hypothesis is presented relating the absence of H2A.F/Z in S. cerevisiae to its function in other organisms.

Download Full-text

The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins.

Molecular and Cellular Biology ◽

10.1128/mcb.5.9.2389 ◽

1985 ◽

Vol 5 (9) ◽

pp. 2389-2398 ◽

Cited By ~ 112

Author(s):

C D Silflow ◽

R L Chisholm ◽

T W Conner ◽

L P Ranum

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Cdna Clones ◽

Gene Products ◽

Beta Tubulin ◽

Alpha Tubulin ◽

Tubulin Genes ◽

Total Complement ◽

Cloned Gene ◽

Net Charges

Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The results predicted that two alpha-tubulin proteins with different net charges are produced as primary gene products. The predicted amino acid sequences are 86 and 70% homologous with alpha-tubulins from rat brain and Schizosaccharomyces pombe, respectively. Each gene had two intervening sequences, located at identical positions. Portions of an intervening sequence highly conserved between the two beta-tubulin genes are also found in the second intervening sequence of each of the alpha genes. These results, together with our earlier report of the beta-tubulin sequences in C. reinhardi, present a picture of the total complement of genetic information for tubulin in this organism.

Download Full-text

GRR1 of Saccharomyces cerevisiae is required for glucose repression and encodes a protein with leucine-rich repeats.

Molecular and Cellular Biology ◽

10.1128/mcb.11.10.5101 ◽

1991 ◽

Vol 11 (10) ◽

pp. 5101-5112 ◽

Cited By ~ 92

Author(s):

J S Flick ◽

M Johnston

Keyword(s):

Saccharomyces Cerevisiae ◽

Protein Interactions ◽

Tandem Repeats ◽

Glucose Repression ◽

Molecular Data ◽

Primary Response ◽

Yeast Cells ◽

Cell Fractionation ◽

Protein Protein Interactions ◽

Yeast Saccharomyces Cerevisiae

Growth of the yeast Saccharomyces cerevisiae on glucose leads to repression of transcription of many genes required for alternative carbohydrate metabolism. The GRR1 gene appears to be of central importance to the glucose repression mechanism, because mutations in GRR1 result in a pleiotropic loss of glucose repression (R. Bailey and A. Woodword, Mol. Gen. Genet. 193:507-512, 1984). We have isolated the GRR1 gene and determined that null mutants are viable and display a number of growth defects in addition to the loss of glucose repression. Surprisingly, grr1 mutations convert SUC2, normally a glucose-repressed gene, into a glucose-induced gene. GRR1 encodes a protein of 1,151 amino acids that is expressed constitutively at low levels in yeast cells. GRR1 protein contains 12 tandem repeats of a sequence similar to leucine-rich motifs found in other proteins that may mediate protein-protein interactions. Indeed, cell fractionation studies are consistent with this view, suggesting that GRR1 protein is tightly associated with a particulate protein fraction in yeast extracts. The combined genetic and molecular data are consistent with the idea that GRR1 protein is a primary response element in the glucose repression pathway and is required for the generation or interpretation of the signal that induces glucose repression.

Download Full-text

SOME FINE STRUCTURE FEATURES OF MEIOSIS IN THE YEAST SACCHAROMYCES CEREVISIAE

Canadian Journal of Genetics and Cytology ◽

10.1139/g71-008 ◽

1971 ◽

Vol 13 (1) ◽

pp. 55-62 ◽

Cited By ~ 6

Author(s):

Ellen Rapport

Keyword(s):

Saccharomyces Cerevisiae ◽

Fine Structure ◽

Light Microscopy ◽

Budding Yeast ◽

Nuclear Organization ◽

Yeast Cells ◽

Yeast Saccharomyces Cerevisiae ◽

Lipid Granules ◽

Meiosis I

Fine structure features of yeast cells in meiosis are reported. Cytoplasmic and nuclear organization are compared during budding, meiosis I and meiosis II. Spindle plaques previously reported in budding yeast are identified during meiosis and the morphology of the plaques in meiosis I and II is illustrated. The dimunition of the vacuole and the increase in the number of lipid, granules in sporulating yeast, known from light microscopy, is confirmed.

Download Full-text

Substitution of histone H3 arginine 72 to alanine leads to deregulation of isoleucine biosynthesis in budding yeast Saccharomyces cerevisiae

Biochemistry and Cell Biology ◽

10.1139/bcb-2020-0651 ◽

2021 ◽

Author(s):

Pilendra Kumar Thakre ◽

Rakesh Kumar Sahu ◽

Raghuvir Singh Tomar

Keyword(s):

Saccharomyces Cerevisiae ◽

Amino Acid ◽

Crucial Role ◽

Minimal Medium ◽

Budding Yeast ◽

Histone H3 ◽

Yeast Cells ◽

Yeast Saccharomyces Cerevisiae ◽

Isoleucine Biosynthesis ◽

Minimal Media

Histone residues play an essential role in the regulation of various biological processes. In the present study, we have utilized the H3/H4 histone mutant library to probe functional aspects of histone residues in amino acid biosynthesis. We found that histone residue H3R72 plays a crucial role in the regulation of isoleucine biosynthesis. Substitution of arginine residue (H3R72) of histone H3 to alanine (H3R72A) renders yeast cells unable to grow in the minimal media. Histone mutant H3R72A requires the external supplementation of either isoleucine, serine, or threonine for the growth in minimal media. We also observed that H3R72 residue and leucine amino acid in synthetic complete media might play a crucial role in determining the intake of isoleucine and threonine in yeast. Further, gene deletion analysis of ILV1 and CHA1 in H3R72A mutant confirmed that isoleucine is the sole requirement for growth in minimal medium. Altogether, we have identified that histone H3R72 residue may be crucial for yeast growth in the minimal medium by regulating isoleucine biosynthesis through the Ilv1 enzyme in budding yeast Saccharomyces cerevisiae.

Download Full-text

The two alpha-tubulin genes of Chlamydomonas reinhardi code for slightly different proteins

Molecular and Cellular Biology ◽

10.1128/mcb.5.9.2389-2398.1985 ◽

1985 ◽

Vol 5 (9) ◽

pp. 2389-2398

Author(s):

C D Silflow ◽

R L Chisholm ◽

T W Conner ◽

L P Ranum

Keyword(s):

Amino Acid ◽

Amino Acid Sequences ◽

Cdna Clones ◽

Gene Products ◽

Beta Tubulin ◽

Alpha Tubulin ◽

Tubulin Genes ◽

Total Complement ◽

Cloned Gene ◽

Net Charges

Full-length cDNA clones corresponding to the transcripts of the two alpha-tubulin genes in Chlamydomonas reinhardi were isolated. DNA sequence analysis of the cDNA clones and cloned gene fragments showed that each gene contains 1,356 base pairs of coding sequence, predicting alpha-tubulin products of 451 amino acids. Of the 27 nucleotide differences between the two genes, only two result in predicted amino acid differences between the two gene products. In the more divergent alpha 2 gene, a leucine replaces an arginine at amino acid 308, and a valine replaces a glycine at amino acid 366. The results predicted that two alpha-tubulin proteins with different net charges are produced as primary gene products. The predicted amino acid sequences are 86 and 70% homologous with alpha-tubulins from rat brain and Schizosaccharomyces pombe, respectively. Each gene had two intervening sequences, located at identical positions. Portions of an intervening sequence highly conserved between the two beta-tubulin genes are also found in the second intervening sequence of each of the alpha genes. These results, together with our earlier report of the beta-tubulin sequences in C. reinhardi, present a picture of the total complement of genetic information for tubulin in this organism.

Download Full-text

Dependence of the yeast Saccharomyces cerevisiae post-reproductive lifespan on the reproductive potential.

Acta Biochimica Polonica ◽

10.18388/abp.2013_1959 ◽

2013 ◽

Vol 60 (1) ◽

Cited By ~ 10

Author(s):

Renata Zadrag-Tecza ◽

Mateusz Molon ◽

Jan Mamczur ◽

Tomasz Bilinski

Keyword(s):

Saccharomyces Cerevisiae ◽

Inverse Relationship ◽

Budding Yeast ◽

Reproductive Potential ◽

Model Organism ◽

Reproductive Stage ◽

Yeast Cells ◽

Yeast Saccharomyces Cerevisiae ◽

Two Stages

The lifespan of budding yeast cells is divided into two stages: reproductive and post-reproductive. The post-reproductive stage of the yeast's lifespan has never been characterized before. We have analyzed the influence of various mutations on the post-reproductive (PRLS) and replicative (RLS) lifespans. The results indicate that PRLS demonstrates an inverse relationship with RLS. The observed lack of differences in the total lifespan (TLS) (expressed in units of time) of strains differing up to five times in RLS (expressed in the number of daughters formed) suggests the necessity of revision of opinions concerning the use of yeast as a model organism of gerontology.

Download Full-text