期刊
BIOCHIMICA ET BIOPHYSICA ACTA-GENE REGULATORY MECHANISMS
卷 1819, 期 9-10, 页码 1098-1106出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbagrm.2011.11.007
关键词
Mitochondrial processing peptidase MPP; Intermediate cleavage peptidase 55 Icp55; Octapeptidylpeptidase 1 Oct1; Inner membrane peptidase IMP; Protein turnover
资金
- Deutsche Forschungsgemeinschaft, Trinationales Graduiertenkolleg [GRK 1478]
- Excellence Initiative of German Federal Government [EXC 294 BIOSS]
- Excellence Initiative of German State Government [EXC 294 BIOSS]
Mitochondrial proteins are synthesized as precursor proteins on either cytosolic or mitochondrial ribosomes. The synthesized precursors from both translation origins possess targeting signals that guide the protein to its final destination in one of the four subcompartments of the organelle. The majority of nuclear-encoded mitochondrial precursors and also mitochondrial-encoded preproteins have an N-terminal presequence that serves as a targeting sequence. Specific presequence peptidases that are found in the matrix, inner membrane and intermembrane space of mitochondria proteolytically remove the signal sequence upon import or sorting. Besides the classical presequence peptidases MPP. IMP and Oct1, several novel proteases have recently been described to possess precursor processing activity, and analysis of their functional relevance revealed a tight connection between precursor processing, mitochondrial dynamics and protein quality control. This article is part of a Special Issue entitled: Mitochondrial Gene Expression. (C) 2011 Elsevier B.V. All rights reserved.
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