, Volume 50, Issue 11–12, pp 1002–1011

Hsp70 in mitochondrial biogenesis: From chaperoning nascent polypeptide chains to facilitation of protein degradation

  • R. A. Stuart
  • D. M. Cyr
  • W. Neupert
Multi-Author Reviews


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, protein translocation across mitochondrial membranes, protein folding and finally the delivery of misfolded proteins to proteolytic enzymes in the mitochondrial matrix.

Key words

Mitochondrial biogenesis nascent polypeptide chains protein translocation matrix-ATP mitochondrial hsp70 molecular chaperones 


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Copyright information

© Birkhäuser Verlag Basel 1994

Authors and Affiliations

  • R. A. Stuart
    • 1
  • D. M. Cyr
    • 1
  • W. Neupert
    • 1
  1. 1.Institut für Physiologische Chemie der Universität MünchenMünchen(Germany)

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