Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria
- PMID: 7913473
- PMCID: PMC2200036
- DOI: 10.1083/jcb.126.2.305
Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria
Abstract
Protein folding in mitochondria is mediated by the chaperonin Hsp60, the homologue of E. coli GroEL. Mitochondria also contain a homologue of the cochaperonin GroES, called Hsp10, which is a functional regulator of the chaperonin. To define the in vivo role of the co-chaperonin, we have used the genetic and biochemical potential of the yeast S. cerevisiae. The HSP10 gene was cloned and sequenced and temperature-sensitive lethal hsp10 mutants were generated. Our results identify Hsp10 as an essential component of the mitochondrial protein folding apparatus, participating in various aspects of Hsp60 function. Hsp10 is required for the folding and assembly of proteins imported into the matrix compartment, and is involved in the sorting of certain proteins, such as the Rieske Fe/S protein, passing through the matrix en route to the intermembrane space. The folding of the precursor of cytosolic dihydrofolate reductase (DHFR), imported into mitochondria as a fusion protein, is apparently independent of Hsp10 function consistent with observations made for the chaperonin-mediated folding of DHFR in vitro. The temperature-sensitive mutations in Hsp10 map to a domain (residues 25-40) that corresponds to a previously identified mobile loop region of bacterial GroES and result in a reduced binding affinity of hsp10 for the chaperonin at the non-permissive temperature.
Similar articles
-
Identification of in vivo substrates of the yeast mitochondrial chaperonins reveals overlapping but non-identical requirement for hsp60 and hsp10.EMBO J. 1998 Oct 15;17(20):5868-76. doi: 10.1093/emboj/17.20.5868. EMBO J. 1998. PMID: 9774331 Free PMC article.
-
Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60.Proc Natl Acad Sci U S A. 1997 Aug 19;94(17):9011-6. doi: 10.1073/pnas.94.17.9011. Proc Natl Acad Sci U S A. 1997. PMID: 9256426 Free PMC article.
-
Roles of molecular chaperones in protein targeting to mitochondria.Philos Trans R Soc Lond B Biol Sci. 1993 Mar 29;339(1289):355-61; discussion 361-2. doi: 10.1098/rstb.1993.0034. Philos Trans R Soc Lond B Biol Sci. 1993. PMID: 8098540 Review.
-
Cloning and disruption of the gene encoding yeast mitochondrial chaperonin 10, the homolog of E. coli groES.FEBS Lett. 1993 Dec 13;335(3):358-60. doi: 10.1016/0014-5793(93)80419-u. FEBS Lett. 1993. PMID: 7903252
-
A mitochondrial chaperonin: genetic, biochemical, and molecular characteristics.Semin Cell Biol. 1990 Feb;1(1):37-45. Semin Cell Biol. 1990. PMID: 1983269 Review.
Cited by
-
Role of Heat Shock Proteins in Atrial Fibrillation: From Molecular Mechanisms to Diagnostic and Therapeutic Opportunities.Cells. 2022 Dec 30;12(1):151. doi: 10.3390/cells12010151. Cells. 2022. PMID: 36611952 Free PMC article. Review.
-
Heat shock proteins and the calcineurin-crz1 signaling regulate stress responses in fungi.Arch Microbiol. 2022 Apr 4;204(5):240. doi: 10.1007/s00203-022-02833-w. Arch Microbiol. 2022. PMID: 35377020 Review.
-
Chemical rescue of mutant proteins in living Saccharomyces cerevisiae cells by naturally occurring small molecules.G3 (Bethesda). 2021 Sep 6;11(9):jkab252. doi: 10.1093/g3journal/jkab252. G3 (Bethesda). 2021. PMID: 34544143 Free PMC article.
-
900 MHz Radiofrequency Field Induces Mitochondrial Unfolded Protein Response in Mouse Bone Marrow Stem Cells.Front Public Health. 2021 Aug 26;9:724239. doi: 10.3389/fpubh.2021.724239. eCollection 2021. Front Public Health. 2021. PMID: 34513791 Free PMC article.
-
The Role of Mitochondrial Dysfunction in Atrial Fibrillation: Translation to Druggable Target and Biomarker Discovery.Int J Mol Sci. 2021 Aug 6;22(16):8463. doi: 10.3390/ijms22168463. Int J Mol Sci. 2021. PMID: 34445167 Free PMC article. Review.
References
Publication types
MeSH terms
Substances
Associated data
- Actions
Grants and funding
LinkOut - more resources
Full Text Sources
Molecular Biology Databases
Research Materials
Miscellaneous