Mitochondrial ATP-independent chaperones

Authors

  • Nikos Petrakis,

    1. Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas (IMBB-FORTH), Heraklion, Crete, Greece
    2. Department of Chemistry, University of Crete, Heraklion, Crete, Greece
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  • Felicity Alcock,

    1. Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas (IMBB-FORTH), Heraklion, Crete, Greece
    Current affiliation:
    1. Department of Biochemistry and Molecular Biology, Monash University, Victoria 3800, Australia
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  • Kostas Tokatlidis

    Corresponding author
    1. Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas (IMBB-FORTH), Heraklion, Crete, Greece
    2. Department of Materials Science and Technology, University of Crete, Heraklion, Crete, Greece
    • Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology Hellas (IMBB-FORTH), Nikolaou Plastira 100, Heraklion 70013, Crete, Greece
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Abstract

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

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