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  GxxxG motifs hold the TIM23 complex together

Demishtein-Zohary, K., Marom, M., Neupert, W., Mokranjac, D., & Azem, A. (2015). GxxxG motifs hold the TIM23 complex together. FEBS JOURNAL, 282(11), 2178-2186. doi:10.1111/febs.13266.

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Demishtein-Zohary, Keren1, Author
Marom, Milit1, Author
Neupert, Walter2, Author              
Mokranjac, Dejana1, Author
Azem, Abdussalam1, Author
Affiliations:
1external, ou_persistent22              
2Neupert, Walter / Structure and Function of Mitochondria, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565163              

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Free keywords: MITOCHONDRIAL PROTEIN IMPORT; INTERMEMBRANE SPACE DOMAIN; SACCHAROMYCES-CEREVISIAE; INNER MEMBRANE; TRANSLOCATION; PRESEQUENCES; PREPROTEINS; MECHANISMS; SUBUNITS; VECTORSimport channel; mitochondrial protein import; Tim17; Tim23; Tim44;
 Abstract: Approximately 99% of the mitochondrial proteome is nucleus-encoded, synthesized in the cytosol, and subsequently imported into and sorted to the correct compartment in the organelle. The translocase of the inner mitochondrial membrane 23 (TIM23) complex is the major protein translocase of the inner membrane, and is responsible for translocation of proteins across the inner membrane and their insertion into the inner membrane. Tim23 is the central component of the complex that forms the import channel. A high-resolution structure of the import channel is still missing, and structural elements important for its function are unknown. In the present study, we analyzed the importance of the highly abundant GxxxG motifs in the transmembrane segments of Tim23 for the structural integrity of the TIM23 complex. Of 10 glycines present in the GxxxG motifs in the first, second and third transmembrane segments of Tim23, mutations of three of them in transmembrane segments 1 and 2 resulted in a lethal phenotype, and mutations of three others in a temperature-sensitive phenotype. The remaining four caused no obvious growth phenotype. Importantly, none of the mutations impaired the import and membrane integration of Tim23 precursor into mitochondria. However, the severity of growth impairment correlated with the destabilization of the TIM23 complex. We conclude that the GxxxG motifs found in the first and second transmembrane segments of Tim23 are necessary for the structural integrity of the TIM23 complex.

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Language(s): eng - English
 Dates: 2015
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000355664000009
DOI: 10.1111/febs.13266
 Degree: -

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Title: FEBS JOURNAL
Source Genre: Journal
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Publ. Info: 111 RIVER ST, HOBOKEN 07030-5774, NJ USA : WILEY-BLACKWELL
Pages: - Volume / Issue: 282 (11) Sequence Number: - Start / End Page: 2178 - 2186 Identifier: ISSN: 1742-464X