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Journal Article

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

MPS-Authors
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Jans,  D. C.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Jakobs,  S.
Research Group of Mitochondrial Structure and Dynamics, MPI for biophysical chemistry, Max Planck Society;

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Lenz,  C.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Urlaub,  H.
Research Group of Bioanalytical Mass Spectrometry, MPI for Biophysical Chemistry, Max Planck Society;

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Fulltext (public)

2351794.pdf
(Publisher version), 710KB

Supplementary Material (public)

2351794_Suppl_1.eps
(Supplementary material), 13MB

2351794_Suppl_2.xlsx
(Supplementary material), 16KB

Citation

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.


Cite as: http://hdl.handle.net/11858/00-001M-0000-002B-9958-6
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.