Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae
@article{Kimura2004TemperaturesensitiveMO, title={Temperature-sensitive mutants of hsp82 of the budding yeast Saccharomyces cerevisiae}, author={Yoko Kimura and Seiji Matsumoto and Ichiro Yahara}, journal={Molecular and General Genetics MGG}, year={2004}, volume={242}, pages={517-527} }
The budding yeast Saccharomyces cerevisiae has two HSP90-related genes per haploid genome, HSP82 and HSC82. Random mutations were induced in vitro in the HSP82 gene by treatment of the plasmid with hydroxylamine. Four temperature-sensitive (ts) mutants and one simultaneously is and cold-sensitivie (cs) mutant were then selected in a yeast strain in which HSC82 had previously been disrupted. The mutants were found to have single base changes in the coding region, which caused single amino acid…
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References
SHOWING 1-10 OF 53 REFERENCES
Mutations of the heat inducible 70 kilodalton genes of yeast confer temperature sensitive growth
- BiologyCell
- 1984
hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.
- BiologyMolecular and cellular biology
- 1989
Biochemical analysis of hsp82 from vertebrate cells suggests that the protein binds to a variety of other cellular proteins, keeping them inactive until they have reached their proper intracellular location or have received the proper activation signal, speculate that the reason cells require higher concentrations of hSP82 or hsc82 for growth at higher temperatures is to maintain proper levels of complex formation with these other proteins.
SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1987
The genome of the yeast Saccharomyces cerevisiae contains a family of genes related to the HSP70 genes (encoding the 70-kDa heat shock protein) of other eukaryotes, and mutations constructed in vitro and substituted into the yeast genome in place of the wild-type alleles indicate that at least three distinct functions are carried out by genes of the H SP70 family.
Hspl04 is a highly conserved protein with two essential nucleotide-binding sites
- BiologyNature
- 1991
Hsp104 is a member of the highly conserved ClpA/ClpB protein family first identified in Escherlchla coli and that additional heat-inducible members of this family are present in Schizosaccharomyces pombe and in mammals.
Complete sequence of the heat shock-inducible HSP90 gene of Saccharomyces cerevisiae.
- BiologyThe Journal of biological chemistry
- 1984
Although the sequences surrounding the coding region of the HSP90 gene are quite similar to those surrounding other sequenced yeast genes, the authors find a limited homology between sequences located 5' to this gene and the putative heat shock-regulatory sequences located5' to the heatshock-inducible genes of Drosophila.
The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation, and other stresses
- BiologyCell
- 1987
Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.
- BiologyProceedings of the National Academy of Sciences of the United States of America
- 1987
The isolation of an E. coli homologue of hsp83 illustrates the remarkable conservation of heat shock proteins in evolution and will facilitate genetic and biochemical experiments aimed at determining the function of hSp83.
Identification and expression of a cloned yeast heat shock gene.
- BiologyThe Journal of biological chemistry
- 1983
Hsp104 is required for tolerance to many forms of stress.
- BiologyThe EMBO journal
- 1992
The hsp104 mutation establishes the validity of a long‐standing hypothesis in the heat‐shock field, namely, that hsps have broadly protective functions and indicates that the underlying causes of lethality are similar in an extraordinary variety of circumstances.
Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae.
- Biology, MedicineMolecular and cellular biology
- 1987
Saccharomyces cerevisiae contains a large family of genes related to hsp70, the major heat shock-inducible gene of Drosophila melanogaster, which indicates that SSA3 encodes a functional protein and that the SSA1, SSA2, S SA3, and SSA4 gene products are functionally similar.