The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.
hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.
Open accessAbstract
hsp82 is one of the most highly conserved and abundantly synthesized heat shock proteins of eucaryotic cells. The yeast Saccharomyces cerevisiae contains two closely related genes in the HSP82 gene family. HSC82 was expressed constitutively at a very high level and was moderately induced by high temperatures. HSP82 was expressed constitutively at a much lower level and was more strongly induced by heat. Site-directed disruption mutations were produced in both genes. Cells homozygous for both mutations did not grow at any temperature. Cells carrying other combinations of the HSP82 and HSC82 mutations grew well at 25 degrees C, but their ability to grow at higher temperatures varied with gene copy number. Thus, HSP82 and HSC82 constitute an essential gene family in yeast cells. Although the two proteins had different patterns of expression, they appeared to have equivalent functions; growth at higher temperatures required higher concentrations of either protein. 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. We 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.
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Metadata
- Authors
- Borkovich, K. A., Farrelly, F. W., Finkelstein, D. B., Taulien, J., & Lindquist, S.
- Affiliations
- Howard Hughes Medical Institute (US)
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1989-09
- Volume
- 9
- Issue
- 9
- Pages
- 3919-3930
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC362454
- OpenAlex
- W1956379070
- Cited by
- 641
- References
- 54
- Citations by year
- 2026: 1 · 2025: 5 · 2024: 22 · 2023: 11 · 2022: 19 · 2021: 16 · 2020: 15 · 2019: 23 · 2018: 16 · 2017: 16 · 2016: 18 · 2015: 11 · 2014: 32 · 2013: 26 · 2012: 24
- FWCI
- 5.41
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of General Medical Sciences (GM 11223, GM3582, GM25829)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Hsp82, heat shock proteins, Saccharomyces cerevisiae, heat tolerance, gene copy number, site-directed mutagenesis, protein-protein complex formation, molecular chaperones, constitutive expression
- MeSH terms
- Amino Acid Sequence, Base Sequence, DNA, Fungal, Gene Expression Regulation, Genes, Fungal, Multigene Family, Hot Temperature, Heat-Shock Proteins, Molecular Sequence Data, Mutation, Saccharomyces cerevisiae, Spores, Fungal
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