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

Journal of cell science | Aug 15, 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.

Pubmed ID: 15280428 RIS Download

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

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Associated grants

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

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