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  TIM29 is a subunit of the human carrier translocase required for protein transport.

Callegari, S., Richter, F., Chojnacka, K., Jans, D. C., Lorenzi, I., Pacheu-Grau, D., et al. (2016). TIM29 is a subunit of the human carrier translocase required for protein transport. FEBS Letters, 590(23), 4147-4158. doi:10.1002/1873-3468.12450.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002B-9958-6 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-9E8F-0
Genre: Journal Article

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 Creators:
Callegari, S., Author
Richter, F., Author
Chojnacka, K., Author
Jans, D. C.1, Author              
Lorenzi, I., Author
Pacheu-Grau, D., Author
Jakobs, S.1, Author              
Lenz, C.2, Author              
Urlaub, H.2, Author              
Dudek, J., Author
Chacinska, A., Author
Rehling, P.3, Author              
Affiliations:
1Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578566              
2Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society, ou_578613              
3Max Planck Fellow Peter Rehling, ou_1298545              

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Free keywords: carrier translocase; membrane protein; mitochondria; protein translocation; TIM22; TIM29
 Abstract: Hydrophobic inner mitochondrial membrane proteins with internal targeting signals, such as the metabolite carriers, use the carrier translocase (TIM22 complex) for transport into the inner membrane. Defects in this transport pathway have been associated with neurodegenerative disorders. While the TIM22 complex is well studied in baker's yeast, very little is known about the mammalian TIM22 complex. Using immunoprecipitation, we purified the human carrier translocase and identified a mitochondrial inner membrane protein TIM29 as a novel component, specific to metazoa. We show that TIM29 is a constituent of the 440 kDa TIM22 complex and interacts with oxidized TIM22. Our analyses demonstrate that TIM29 is required for the structural integrity of the TIM22 complex and for import of substrate proteins by the carrier translocase. This article is protected by copyright. All rights reserved.

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Language(s): eng - English
 Dates: 2016-10-262016-12
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1002/1873-3468.12450
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Title: FEBS Letters
Source Genre: Journal
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Pages: - Volume / Issue: 590 (23) Sequence Number: - Start / End Page: 4147 - 4158 Identifier: -