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JCS ePress
online publication date 27 Jul 2004
doi: 10.1242/jcs.01275
Research Article
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*
* Author for correspondence (e-mail: ron{at}saturn.med.nyu.ed)
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.

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