Literature DB >> 2674684

hsp82 is an essential protein that is required in higher concentrations for growth of cells at higher temperatures.

K A Borkovich1, F W Farrelly, D B Finkelstein, J Taulien, S Lindquist.   

Abstract

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.

Entities:  

Mesh:

Substances:

Year:  1989        PMID: 2674684      PMCID: PMC362454          DOI: 10.1128/mcb.9.9.3919-3930.1989

Source DB:  PubMed          Journal:  Mol Cell Biol        ISSN: 0270-7306            Impact factor:   4.272


  42 in total

1.  Principles of protein-protein recognition.

Authors:  C Chothia; J Janin
Journal:  Nature       Date:  1975-08-28       Impact factor: 49.962

2.  Nucleotide sequence of a cDNA for a member of the human 90-kDa heat-shock protein family.

Authors:  N F Rebbe; J Ware; R M Bertina; P Modrich; D W Stafford
Journal:  Gene       Date:  1987       Impact factor: 3.688

3.  The specific interaction of the Rous sarcoma virus transforming protein, pp60src, with two cellular proteins.

Authors:  J S Brugge; E Erikson; R L Erikson
Journal:  Cell       Date:  1981-08       Impact factor: 41.582

4.  Transit of pp60v-src to the plasma membrane.

Authors:  S A Courtneidge; J M Bishop
Journal:  Proc Natl Acad Sci U S A       Date:  1982-12       Impact factor: 11.205

5.  One-step gene disruption in yeast.

Authors:  R J Rothstein
Journal:  Methods Enzymol       Date:  1983       Impact factor: 1.600

6.  A regulatory upstream promoter element in the Drosophila hsp 70 heat-shock gene.

Authors:  H R Pelham
Journal:  Cell       Date:  1982-09       Impact factor: 41.582

7.  Rapid DNA isolations for enzymatic and hybridization analysis.

Authors:  R W Davis; M Thomas; J Cameron; T P St John; S Scherer; R A Padgett
Journal:  Methods Enzymol       Date:  1980       Impact factor: 1.600

8.  The structure of transposable yeast mating type loci.

Authors:  K A Nasmyth; K Tatchell
Journal:  Cell       Date:  1980-03       Impact factor: 41.582

9.  Transformation of intact yeast cells treated with alkali cations.

Authors:  H Ito; Y Fukuda; K Murata; A Kimura
Journal:  J Bacteriol       Date:  1983-01       Impact factor: 3.490

10.  Molecular cloning and expression of a gene that controls the high-temperature regulon of Escherichia coli.

Authors:  F C Neidhardt; R A VanBogelen; E T Lau
Journal:  J Bacteriol       Date:  1983-02       Impact factor: 3.490

View more
  264 in total

1.  Cell cycle transition under stress conditions controlled by vertebrate heat shock factors.

Authors:  A Nakai; T Ishikawa
Journal:  EMBO J       Date:  2001-06-01       Impact factor: 11.598

Review 2.  HSP90 at the hub of protein homeostasis: emerging mechanistic insights.

Authors:  Mikko Taipale; Daniel F Jarosz; Susan Lindquist
Journal:  Nat Rev Mol Cell Biol       Date:  2010-06-09       Impact factor: 94.444

3.  Role of HSP90 in salt stress tolerance via stabilization and regulation of calcineurin.

Authors:  J Imai; I Yahara
Journal:  Mol Cell Biol       Date:  2000-12       Impact factor: 4.272

4.  Uncoupling gene activity from chromatin structure: promoter mutations can inactivate transcription of the yeast HSP82 gene without eliminating nucleosome-free regions.

Authors:  M S Lee; W T Garrard
Journal:  Proc Natl Acad Sci U S A       Date:  1992-10-01       Impact factor: 11.205

5.  Cytosolic HSP90 associates with and modulates the Arabidopsis RPM1 disease resistance protein.

Authors:  David A Hubert; Pablo Tornero; Youssef Belkhadir; Priti Krishna; Akira Takahashi; Ken Shirasu; Jeffery L Dangl
Journal:  EMBO J       Date:  2003-11-03       Impact factor: 11.598

6.  Control of Hsp90 chaperone and its clients by N-terminal acetylation and the N-end rule pathway.

Authors:  Jang-Hyun Oh; Ju-Yeon Hyun; Alexander Varshavsky
Journal:  Proc Natl Acad Sci U S A       Date:  2017-05-17       Impact factor: 11.205

Review 7.  New developments in Hsp90 inhibitors as anti-cancer therapeutics: mechanisms, clinical perspective and more potential.

Authors:  Yanyan Li; Tao Zhang; Steven J Schwartz; Duxin Sun
Journal:  Drug Resist Updat       Date:  2009 Feb-Apr       Impact factor: 18.500

8.  Alteration of the protein kinase binding domain enhances function of the Saccharomyces cerevisiae molecular chaperone Cdc37.

Authors:  Min Ren; Arti Santhanam; Paul Lee; Avrom Caplan; Stephen Garrett
Journal:  Eukaryot Cell       Date:  2007-06-15

9.  Developmental expression of tomato heat-shock cognate protein 80.

Authors:  A J Koning; R Rose; L Comai
Journal:  Plant Physiol       Date:  1992-10       Impact factor: 8.340

10.  Identification of SSF1, CNS1, and HCH1 as multicopy suppressors of a Saccharomyces cerevisiae Hsp90 loss-of-function mutation.

Authors:  D F Nathan; M H Vos; S Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  1999-02-16       Impact factor: 11.205

View more

北京卡尤迪生物科技股份有限公司 © 2022-2023.