doi: 10.1128/jb.170.7.2977-2983.1988.
Ancient heat shock gene is dispensable
Affiliations
- PMID: 3290192
- PMCID: PMC211237
- DOI: 10.1128/jb.170.7.2977-2983.1988
Item in Clipboard
Ancient heat shock gene is dispensable
J Bacteriol.
1988 Jul.
Erratum in
- J Bacteriol 1988 Oct;170(10):4999
Abstract
Hsp83 is a major eucaryotic heat shock protein and one of the most conserved proteins known. We have isolated an Escherichia coli gene homologous to eucaryotic Hsp83 and used it to construct a deletion mutation. The E. coli mutant was viable but had a slight growth disadvantage that increased with temperature.
Similar articles
-
Isolation and characterization of Escherichia coli mutants that lack the heat shock sigma factor sigma 32.J Bacteriol. 1988 Aug;170(8):3640-9. doi: 10.1128/jb.170.8.3640-3649.1988. J Bacteriol. 1988. PMID: 2900239 Free PMC article.
-
The heat-shock-regulated grpE gene of Escherichia coli is required for bacterial growth at all temperatures but is dispensable in certain mutant backgrounds.J Bacteriol. 1989 May;171(5):2748-55. doi: 10.1128/jb.171.5.2748-2755.1989. J Bacteriol. 1989. PMID: 2651417 Free PMC article.
-
Escherichia coli dnaK null mutants are inviable at high temperature.J Bacteriol. 1987 Jan;169(1):283-90. doi: 10.1128/jb.169.1.283-290.1987. J Bacteriol. 1987. PMID: 3025174 Free PMC article.
-
Eukaryotic Mr 83,000 heat shock protein has a homologue in Escherichia coli.Proc Natl Acad Sci U S A. 1987 Aug;84(15):5177-81. doi: 10.1073/pnas.84.15.5177. Proc Natl Acad Sci U S A. 1987. PMID: 3299380 Free PMC article.
-
The genetics and regulation of heat-shock proteins.Annu Rev Genet. 1984;18:295-329. doi: 10.1146/annurev.ge.18.120184.001455. Annu Rev Genet. 1984. PMID: 6442118 Review. No abstract available.
Cited by
-
The recR locus of Escherichia coli K-12: molecular cloning, DNA sequencing and identification of the gene product.Nucleic Acids Res. 1989 Sep 12;17(17):6781-94. doi: 10.1093/nar/17.17.6781. Nucleic Acids Res. 1989. PMID: 2674903 Free PMC article.
-
Physical interaction between bacterial heat shock protein (Hsp) 90 and Hsp70 chaperones mediates their cooperative action to refold denatured proteins.J Biol Chem. 2014 Feb 28;289(9):6110-9. doi: 10.1074/jbc.M113.524801. Epub 2014 Jan 12. J Biol Chem. 2014. PMID: 24415765 Free PMC article.
-
Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase.Mol Cell Biol. 1995 Jul;15(7):3917-25. doi: 10.1128/MCB.15.7.3917. Mol Cell Biol. 1995. PMID: 7791797 Free PMC article.
-
ATP binding to Hsp90 is sufficient for effective chaperoning of p53 protein.J Biol Chem. 2010 Oct 15;285(42):32020-8. doi: 10.1074/jbc.M110.112110. Epub 2010 Aug 5. J Biol Chem. 2010. PMID: 20688913 Free PMC article.
-
Regulation of the Bacillus subtilis heat shock gene htpG is under positive control.J Bacteriol. 2003 Jan;185(2):466-74. doi: 10.1128/JB.185.2.466-474.2003. J Bacteriol. 2003. PMID: 12511492 Free PMC article.
References
Publication types
MeSH terms
Substances
Grants and funding
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases
