期刊
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
卷 1823, 期 7, 页码 1142-1150出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2012.04.014
关键词
Disulfide bond formation and transfer; Erv1; Mia40; Protein import; Protein translocation; Redox
资金
- Australian Research Council
- Clive and Vera Ramaciotti Foundation
- National Health and Medical Research Council
- Foundation for Polish Science Welcome Programme
- EU within European Regional Development Fund
- EMBO Installation grant
- Ministry of Science and Higher Education in Poland [NN301 298337]
Many newly synthesized proteins obtain disulfide bonds in the bacterial periplasm, the endoplasmic reticulum (ER) and the mitochondrial intermembrane space. The acquisition of disulfide bonds is critical for the folding, assembly and activity of these proteins. Spontaneous oxidation of thiol groups is inefficient in vivo, therefore cells have developed machineries that catalyse the oxidation of substrate proteins. The identification of the machinery that mediates this process in the intermembrane space of mitochondria, known as MIA (mitochondrial intermembrane space assembly), provided a unique mechanism of protein transport. The MIA machinery introduces disulfide bonds into incoming intermembrane space precursors and thus tightly couples the process of precursor translocation to precursor oxidation. We discuss our current understanding of the MIA pathway and the mechanisms that oversee thiol-exchange reactions in mitochondria. (C) 2012 Elsevier B.V. All rights reserved.
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