Hsp70 in mitochondrial biogenesis: from chaperoning nascent polypeptide chains to facilitation of protein degradation.
The family of hsp70 (70 kilodalton heat shock protein) molecular chaperones plays an essential and diverse role in cellular physiology. Hsp70 proteins appear to elicit their effects by interacting with polypeptides that present domains which exhibit non-native conformations at distinct stages during their life in the cell. In this paper we review work pertaining to the functions of hsp70 proteins in chaperoning mitochondrial protein biogenesis. Hsp70 proteins function in protein synthesis, proteins to proteolytic enzymes in the mitochondrial matrix.
Stuart
R A
RA
Institut für Physiologische Chemie, Universität München, Germany.
Cyr
D M
DM
Neupert
W
W
D000818:Animals; D001692:Biological Transport; D004272:DNA, Mitochondrial / Q000378:metabolism; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D006801:Humans; D008928:Mitochondria / Q000378:metabolism*; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*
D004272:DNA, Mitochondrial; D018840:HSP70 Heat-Shock Proteins; D011506:Proteins