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Mitochondrial ATP‐independent chaperones
Author(s) -
Petrakis Nikos,
Alcock Felicity,
Tokatlidis Kostas
Publication year - 2009
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.235
Subject(s) - intermembrane space , mitochondrial intermembrane space , chaperone (clinical) , translocase of the outer membrane , translocase of the inner membrane , microbiology and biotechnology , mitochondrion , mitochondrial carrier , atp–adp translocase , inner membrane , inner mitochondrial membrane , chemistry , biology , bacterial outer membrane , biochemistry , mitochondrial membrane transport protein , gene , escherichia coli , medicine , pathology
Mitochondria possess a dedicated‐chaperone system in the intermembrane space, the small Tims that are ubiquitous in all eukaryotes from yeast to man. They escort membrane proteins to the outer or the inner membrane for proper insertion. These mitochondrial chaperones do not require external energy to perform their function and have structural similarities to other ATP‐independent chaperones. Here, we discuss their structural properties and how these relate to their chaperoning function in the mitochondrial intermembrane space. © 2009 IUBMB IUBMB Life 61(9): 909–914, 2009