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

Bajaj, R., Munari, F., Becker, S., & Zweckstetter, M. (2014). Interaction of the intermembrane space domain of Tim23 protein with mitochondrial membranes. Journal of Biological Chemistry, 289(50), 34620-34626. doi:10.1074/jbc.M114.595702.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0024-651C-3 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-D0C1-F
Genre: Journal Article

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 Creators:
Bajaj, R.1, Author              
Munari, F.1, Author              
Becker, S.2, Author              
Zweckstetter, M.1, Author              
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

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Free keywords: Lipid; Membrane; Mitochondria; Nuclear Magnetic Resonance (NMR); Protein Translocation; Protein Import
 Abstract: Background: Tim23 mediates protein translocation into mitochondria. Results: Tim23 binds to mitochondria-like membranes through a hydrophobic anchor at its N terminus, with cardiolipin enhancing the interaction. Conclusion: The intermembrane space domain of Tim23 can interact with both inner and outer mitochondria-like membranes. Significance: Tim23 provides the central element for formation of the translocation contact. 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.

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Language(s): eng - English
 Dates: 2014-10-272014-12-12
 Publication Status: Published in print
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.M114.595702
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 289 (50) Sequence Number: - Start / End Page: 34620 - 34626 Identifier: -