Literature DB >> 1983269

A mitochondrial chaperonin: genetic, biochemical, and molecular characteristics.

R L Hallberg1.   

Abstract

Mitochondria contain a matrix-localized protein complex composed of subunits homologous to the E.coli protein groEL. As with groEL in E.coli, the nuclear gene coding for the mitochondrial protein is essential for cell survival and the accumulation of the protein is elevated at heat shock-inducing temperatures. Biochemical analyses of wild type and mutant yeast strains have shown that this protein, hsp60, is required for the correct folding and assembly of newly imported, mitochondrially-targeted proteins. There is evidence suggesting a mandatory interaction between hsp60 and many imported, as well as mitochondrially-synthesized, proteins. The implications of these and other data are discussed.

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Year:  1990        PMID: 1983269

Source DB:  PubMed          Journal:  Semin Cell Biol        ISSN: 1043-4682


  3 in total

1.  Inhibitory effects of HSP70 chaperones on nascent polypeptides.

Authors:  C Ryan; T H Stevens; M J Schlesinger
Journal:  Protein Sci       Date:  1992-08       Impact factor: 6.725

2.  Synaptophysin-containing microvesicles transport heat-shock protein hsp60 in insulin-secreting beta cells.

Authors:  K Brudzynski; V Martinez
Journal:  Cytotechnology       Date:  1993       Impact factor: 2.058

3.  Immunocytochemical localization of heat-shock protein 60-related protein in beta-cell secretory granules and its altered distribution in non-obese diabetic mice.

Authors:  K Brudzynski; V Martinez; R S Gupta
Journal:  Diabetologia       Date:  1992-04       Impact factor: 10.122

  3 in total

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