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First published online 27 July 2004
doi: 10.1242/jcs.01275

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Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones

Takunari Yoneda^*,, Cristina Benedetti^*, Fumihiko Urano, Scott G. Clark, Heather P. Harding and David Ron^¶

Skirball Institute of Biomolecular Medicine and the Departments of Cell Biology and Medicine, New York University School of Medicine, 540 First Avenue, New York, NY 10016, USA

^¶ Author for correspondence (e-mail: ron{at}saturn.med.nyu.ed)

Accepted 19 April 2004

Protein folding in the mitochondria is assisted by nuclear-encoded compartment-specific chaperones but regulation of the expression of their encoding genes is poorly understood. We found that the mitochondrial matrix HSP70 and HSP60 chaperones, encoded by the Caenorhabditis elegans hsp-6 and hsp-60 genes, were selectively activated by perturbations that impair assembly of multi-subunit mitochondrial complexes or by RNAi of genes encoding mitochondrial chaperones or proteases, which lead to defective protein folding and processing in the organelle. hsp-6 and hsp-60 induction was specific to perturbed mitochondrial protein handling, as neither heat-shock nor endoplasmic reticulum stress nor manipulations that impair mitochondrial steps in intermediary metabolism or ATP synthesis activated the mitochondrial chaperone genes. These observations support the existence of a mitochondrial unfolded protein response that couples mitochondrial chaperone gene expression to changes in the protein handling environment in the organelle.

Key words: Protein folding, Chaperones, Organelle, Signaling, Genetics

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