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Biochim Biophys Acta. 2013 Feb;1833(2):388-99. doi: 10.1016/j.bbamcr.2012.06.005. Epub 2012 Jun 13.

Chaperone-protease networks in mitochondrial protein homeostasis.

Author information

1
Institut für Biochemie und Molekularbiologie IBMB, Universität Bonn, Nussallee 11, 53115 Bonn, Germany. wolfgang.voos@uni-bonn.de

Abstract

As essential organelles, mitochondria are intimately integrated into the metabolism of a eukaryotic cell. The maintenance of the functional integrity of the mitochondrial proteome, also termed protein homeostasis, is facing many challenges both under normal and pathological conditions. First, since mitochondria are derived from bacterial ancestor cells, the proteins in this endosymbiotic organelle have a mixed origin. Only a few proteins are encoded on the mitochondrial genome, most genes for mitochondrial proteins reside in the nuclear genome of the host cell. This distribution requires a complex biogenesis of mitochondrial proteins, which are mostly synthesized in the cytosol and need to be imported into the organelle. Mitochondrial protein biogenesis usually therefore comprises complex folding and assembly processes to reach an enzymatically active state. In addition, specific protein quality control (PQC) processes avoid an accumulation of damaged or surplus polypeptides. Mitochondrial protein homeostasis is based on endogenous enzymatic components comprising a diverse set of chaperones and proteases that form an interconnected functional network. This review describes the different types of mitochondrial proteins with chaperone functions and covers the current knowledge of their roles in protein biogenesis, folding, proteolytic removal and prevention of aggregation, the principal reactions of protein homeostasis. This article is part of a Special Issue entitled: Protein Import and Quality Control in Mitochondria and Plastids.

PMID:
22705353
DOI:
10.1016/j.bbamcr.2012.06.005
[Indexed for MEDLINE]
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