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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. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.


Rakhi Bajaj, Francesca Munari, Stefan Becker, Markus Zweckstetter. Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes. The Journal of biological chemistry. 2014 Dec 12;289(50):34620-6

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PMID: 25349212

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