ArticleProceedings of the National Academy of Sciences of the United States of America1996
Two eukaryote-specific regions of Hsp82 are dispensable for its viability and signal transduction functions in yeast.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 112 citations in OpenAlex.
- Beyond a Passive Tether: Structural Insights into the Disordered Tail of Hsp90.Journal of the American Chemical Society · 2026Article
- C-terminal domain dimerization in yeast Hsp90 is moderately modulated by the other domains.Biophysical journal · 2024Article
- DNA damage-induced nuclear import of HSP90α is promoted by Aha1.Molecular biology of the cell · 2022Article
- Article
- Disrupting progression of the yeast Hsp90 folding pathway at different transition points results in client-specific maturation defects.Genetics · 2021Article
- Structural elements in the flexible tail of the co-chaperone p23 coordinate client binding and progression of the Hsp90 chaperone cycle.Nature communications · 2021Article
- Article
- The HSP90 Family: Structure, Regulation, Function, and Implications in Health and Disease.International journal of molecular sciences · 2018Review
- A chemical compound inhibiting the Aha1-Hsp90 chaperone complex.The Journal of biological chemistry · 2017Article
- Hop/Sti1 phosphorylation inhibits its co-chaperone function.EMBO reports · 2015Article
- Both the charged linker region and ATPase domain of Hsp90 are essential for Rad51-dependent DNA repair.Eukaryotic cell · 2015Article
- Human, vector and parasite Hsp90 proteins: A comparative bioinformatics analysis.FEBS open bio · 2015Article
- The Hsp90 cochaperones Cpr6, Cpr7, and Cns1 interact with the intact ribosome.Eukaryotic cell · 2015Article
- The charged linker of the molecular chaperone Hsp90 modulates domain contacts and biological function.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Mutation of essential Hsp90 co-chaperones SGT1 or CNS1 renders yeast hypersensitive to overexpression of other co-chaperones.Current genetics · 2014Article
- Uncovering a region of heat shock protein 90 important for client binding in E. coli and chaperone function in yeast.Molecular cell · 2013Article
- Solubility-promoting function of Hsp90 contributes to client maturation and robust cell growth.Eukaryotic cell · 2012Article
- Chaperoning the chaperone: a role for the co-chaperone Cpr7 in modulating Hsp90 function in Saccharomyces cerevisiae.Genetics · 2012Article
- The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.The EMBO journal · 2012Article
- Secreted heat shock protein-90 (Hsp90) in wound healing and cancer.Biochimica et biophysica acta · 2012Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that is very abundant even at normal temperature. It is highly conserved and essential for viability in yeast. To delineate functional domains of Hsp90, we have performed a deletion analysis of one of the two Hsp90 isoforms from budding yeast, Hsp82. The Hsp82 derivatives were tested for complementation of a Hsp90-deficient yeast strain and for their ability to function in two signal transduction pathways that depend on Hsp90. Surprisingly, we found that two salient features of Hsp90 sequences from eukaryotes, the N-terminal charged domain and the extremely conserved C-terminal pentapeptide MEEVD, are dispensable for viability as well as for proper regulation of vertebrate steroid receptors and for pheromone signaling. Moreover, we describe, to our knowledge, the first dominant negative mutant of Hsp90; A Hsp82 derivative that lacks amino acids 538-552 fails to complement but has a dominant negative effect on viability of wild-type strains at moderately elevated temperatures. This mutant may become a valuable tool to study Hsp90 functions both in yeast and in mammalian cells.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.