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

DOI PDF 被引用文献6件
  • Takunari Yoneda
    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
  • Cristina Benedetti
    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
  • Fumihiko Urano
    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
  • Scott G. Clark
    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
  • Heather P. Harding
    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
  • 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

書誌事項

公開日
2004-08-15
DOI
  • 10.1242/jcs.01275
公開者
The Company of Biologists

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説明

<jats:p>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.</jats:p>

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