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Processing of mitochondrial presequences.

Authors: Mossmann, D  Meisinger, C  Vogtle, FN 
Citation: Mossmann D, etal., Biochim Biophys Acta. 2012 Sep-Oct;1819(9-10):1098-106. doi: 10.1016/j.bbagrm.2011.11.007. Epub 2011 Dec 7.
Pubmed: (View Article at PubMed) PMID:22172993
DOI: Full-text: DOI:10.1016/j.bbagrm.2011.11.007

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.


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RGD ID: 10412669
Created: 2015-11-19
Species: All species
Last Modified: 2015-11-19
Status: ACTIVE


RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.