Compartment-specific perturbation of protein handling activates genes encoding mitochondrial chaperones
Authors
Yoneda, TakunariBenedetti, Cristina
Urano, Fumihiko
Clark, Scott G.
Harding, Heather P.
Ron, David
Document Type
Journal ArticlePublication Date
2004-07-29Keywords
AnimalsCaenorhabditis 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
Genetics and Genomics
Metadata
Show full item recordAbstract
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.Source
J Cell Sci. 2004 Aug 15;117(Pt 18):4055-66. Epub 2004 Jul 27. Link to article on publisher's siteDOI
10.1242/jcs.01275Permanent Link to this Item
http://hdl.handle.net/20.500.14038/43929PubMed ID
15280428Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1242/jcs.01275