Abstract
Disruption of protein homeostasis in mitochondria elicits a cellular response, which upregulates mitochondrial chaperones and other factors that serve to remodel the mitochondrial-folding environment. In a recent study, Haynes and colleagues uncovered a novel signal transduction pathway underlying this process. The upstream mitochondrial component of this pathway is an orthologue of Escherichia coli ClpP, which functions in the bacterial heat-shock response. These findings suggest that molecular aspects of stress sensing might be conserved between bacteria and mitochondria.
MeSH terms
-
Animals
-
Bacterial Physiological Phenomena
-
Caenorhabditis elegans / genetics
-
Caenorhabditis elegans / metabolism
-
Caenorhabditis elegans / physiology*
-
Caenorhabditis elegans Proteins / genetics
-
Caenorhabditis elegans Proteins / metabolism
-
Endopeptidase Clp / genetics
-
Endopeptidase Clp / metabolism
-
Gene Expression Regulation
-
Heat-Shock Proteins / genetics
-
Heat-Shock Proteins / metabolism
-
Mitochondria / physiology*
-
Molecular Chaperones / genetics
-
Molecular Chaperones / metabolism
-
Protein Folding*
-
Signal Transduction*
-
Ubiquitins / genetics
-
Ubiquitins / metabolism
Substances
-
Caenorhabditis elegans Proteins
-
Heat-Shock Proteins
-
Molecular Chaperones
-
Ubiquitins
-
Ubl-5 protein, C elegans
-
Endopeptidase Clp