QUICK SEARCH:   [advanced] Author: Keyword(s):
Home     Help     Feedback     Subscriptions     Archive     Search     Table of Contents

First published online 27 July 2004
doi: 10.1242/jcs.01275

This Article Figures Only Full Text Full Text (PDF) Supplemental Data All Versions of this Article: jcs.01275v1 117/18/4055    most recent Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Yoneda, T. Articles by Ron, D. Search for Related Content PubMed PubMed Citation Articles by Yoneda, T. Articles by Ron, D.

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^¶

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

^¶ Author for correspondence (e-mail: ron{at}saturn.med.nyu.ed)

Accepted 19 April 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.

Key words: Protein folding, Chaperones, Organelle, Signaling, Genetics

This article has been cited by other articles:

				S. Zuryn, J. Kuang, and P. Ebert Mitochondrial Modulation of Phosphine Toxicity and Resistance in Caenorhabditis elegans Toxicol. Sci., March 1, 2008; 102(1): 179 - 186. [Abstract] [Full Text] [PDF]

				D. D. Arrington and R. G. Schnellmann Targeting of the molecular chaperone oxygen-regulated protein 150 (ORP150) to mitochondria and its induction by cellular stress Am J Physiol Cell Physiol, February 1, 2008; 294(2): C641 - C650. [Abstract] [Full Text] [PDF]

				C. Benedetti, C. M. Haynes, Y. Yang, H. P. Harding, and D. Ron Ubiquitin-Like Protein 5 Positively Regulates Chaperone Gene Expression in the Mitochondrial Unfolded Protein Response Genetics, September 1, 2006; 174(1): 229 - 239. [Abstract] [Full Text] [PDF]

				B. Hamilton, Y. Dong, M. Shindo, W. Liu, I. Odell, G. Ruvkun, and S. S. Lee A systematic RNAi screen for longevity genes in C. elegans Genes & Dev., July 1, 2005; 19(13): 1544 - 1555. [Abstract] [Full Text] [PDF]

				S. Augustin, M. Nolden, S. Muller, O. Hardt, I. Arnold, and T. Langer Characterization of Peptides Released from Mitochondria: EVIDENCE FOR CONSTANT PROTEOLYSIS AND PEPTIDE EFFLUX J. Biol. Chem., January 28, 2005; 280(4): 2691 - 2699. [Abstract] [Full Text] [PDF]