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J Biol Chem. 2014 Dec 12;289(50):34620-6. doi: 10.1074/jbc.M114.595702. Epub 2014 Oct 27.

Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes.

Author information

1
From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and.
2
From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and the German Center for Neurodegenerative Diseases (DZNE), 37077 Göttingen and.
3
From the Department of NMR-based Structural Biology, Max Planck Institute for Biophysical Chemistry and the German Center for Neurodegenerative Diseases (DZNE), 37077 Göttingen and the Center for Nanoscale Microscopy and Molecular Physiology of the Brain (CNMPB), University Medicine Göttingen, 37073 Göttingen, Germany markus.zweckstetter@dzne.de.

Abstract

Tim23 mediates protein translocation into mitochondria. Although inserted into the inner membrane, the dynamic association of its intermembrane space (IMS) domain with the outer membrane promotes protein import. However, little is known about the molecular basis of this interaction. Here, we demonstrate that the IMS domain of Tim23 tightly associates with both inner and outer mitochondrial membrane-like membranes through a hydrophobic anchor at its N terminus. The structure of membrane-bound Tim23(IMS) is highly dynamic, allowing recognition of both the incoming presequence and other translocase components at the translocation contact. Cardiolipin enhances Tim23 membrane attachment, suggesting that cardiolipin can influence preprotein import.

KEYWORDS:

Lipid; Membrane; Mitochondria; Nuclear Magnetic Resonance (NMR); Protein Import; Protein Translocation

PMID:
25349212
PMCID:
PMC4263868
DOI:
10.1074/jbc.M114.595702
[Indexed for MEDLINE]
Free PMC Article

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