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. 1994 Nov;127(4):893-902.
doi: 10.1083/jcb.127.4.893.

Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA

J M Herrmann  1 , R A Stuart, E A Craig, W Neupert
Affiliations

Mitochondrial heat shock protein 70, a molecular chaperone for proteins encoded by mitochondrial DNA

J M Herrmann et al. J Cell Biol. 1994 Nov.

Abstract

Mitochondrial heat shock protein 70 (mt-Hsp70) has been shown to play an important role in facilitating import into, as well as folding and assembly of nuclear-encoded proteins in the mitochondrial matrix. Here, we describe a role for mt-Hsp70 in chaperoning proteins encoded by mitochondrial DNA and synthesized within mitochondria. The availability of mt-Hsp70 function influences the pattern of proteins synthesized in mitochondria of yeast both in vivo and in vitro. In particular, we show that mt-Hsp70 acts in maintaining the var1 protein, the only mitochondrially encoded subunit of mitochondrial ribosomes, in an assembly competent state, especially under heat stress conditions. Furthermore, mt-Hsp70 helps to facilitate assembly of mitochondrially encoded subunits of the ATP synthase complex. By interacting with the ATP-ase 9 oligomer, mt-Hsp70 promotes assembly of ATP-ase 6, and thereby protects the latter protein from proteolytic degradation. Thus mt-Hsp70 by acting as a chaperone for proteins encoded by the mitochondrial DNA, has a critical role in the assembly of supra-molecular complexes.

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References

    1. Nature. 1970 Aug 15;227(5259):680-5 - PubMed
    1. FEBS Lett. 1990 Jul 30;268(1):265-8 - PubMed
    1. FEBS Lett. 1993 Aug 23;329(1-2):47-50 - PubMed
    1. Biochim Biophys Acta. 1973 Feb 12;301(1):71-104 - PubMed
    1. J Biol Chem. 1993 Nov 15;268(32):23751-4 - PubMed

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