, Volume 50, Issue 11, pp 1002–1011

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


  • R. A. Stuart
    • Institut für Physiologische Chemie der Universität München
  • D. M. Cyr
    • Institut für Physiologische Chemie der Universität München
  • W. Neupert
    • Institut für Physiologische Chemie der Universität München
Multi-Author Reviews

DOI: 10.1007/BF01923454

Cite this article as:
Stuart, R.A., Cyr, D.M. & Neupert, W. Experientia (1994) 50: 1002. doi:10.1007/BF01923454


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 biogenesisnascent polypeptide chainsprotein translocationmatrix-ATPmitochondrial hsp70molecular chaperones

Copyright information

© Birkhäuser Verlag Basel 1994