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

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.

Pubmed ID: 15280428


  • Yoneda T
  • Benedetti C
  • Urano F
  • Clark SG
  • Harding HP
  • Ron D


Journal of cell science

Publication Data

August 15, 2004

Associated Grants

  • Agency: NIDDK NIH HHS, Id: DK47119
  • Agency: NIEHS NIH HHS, Id: ES08681

Mesh Terms

  • Animals
  • Caenorhabditis elegans
  • Cell Compartmentation
  • Chaperonin 60
  • Endoplasmic Reticulum
  • Energy Metabolism
  • Gene Expression Regulation
  • HSP70 Heat-Shock Proteins
  • Heat-Shock Response
  • Intracellular Membranes
  • Macromolecular Substances
  • Mitochondria
  • Molecular Chaperones
  • Oxidative Stress
  • Protein Folding
  • RNA Interference
  • Transcriptional Activation