Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria

Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner...

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Main Authors:	Tamura, Yasushi, Harada, Yoshihiro, Yamano, Koji, Watanabe, Kazuaki, Ishikawa, Daigo, Ohshima, Chié, Nishikawa, Shuh-ichi, Yamamoto, Hayashi, Endo, Toshiya
Format:	Online
Language:	English
Published:	The Rockefeller University Press 2006
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064306/

id	pubmed-2064306
recordtype	oai_dc
spelling	pubmed-20643062007-11-29 Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria Tamura, Yasushi Harada, Yoshihiro Yamano, Koji Watanabe, Kazuaki Ishikawa, Daigo Ohshima, Chié Nishikawa, Shuh-ichi Yamamoto, Hayashi Endo, Toshiya Research Articles Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner mitochondrial membrane protein facing the matrix. Disruption of the TAM41 gene led to temperature-sensitive growth of yeast cells and resulted in defects in protein import via the TIM23 translocator complex at elevated temperature both in vivo and in vitro. Although Tam41 is not a constituent of the TIM23 complex, depletion of Tam41 led to a decreased molecular size of the TIM23 complex and partial aggregation of Pam18 and -16. Import of Pam16 into mitochondria without Tam41 was retarded, and the imported Pam16 formed aggregates in vitro. These results suggest that Tam41 facilitates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex from the matrix side of the inner membrane. The Rockefeller University Press 2006-08-28 /pmc/articles/PMC2064306/ /pubmed/16943180 http://dx.doi.org/10.1083/jcb.200603087 Text en Copyright © 2006, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Tamura, Yasushi Harada, Yoshihiro Yamano, Koji Watanabe, Kazuaki Ishikawa, Daigo Ohshima, Chié Nishikawa, Shuh-ichi Yamamoto, Hayashi Endo, Toshiya
spellingShingle	Tamura, Yasushi Harada, Yoshihiro Yamano, Koji Watanabe, Kazuaki Ishikawa, Daigo Ohshima, Chié Nishikawa, Shuh-ichi Yamamoto, Hayashi Endo, Toshiya Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
author_facet	Tamura, Yasushi Harada, Yoshihiro Yamano, Koji Watanabe, Kazuaki Ishikawa, Daigo Ohshima, Chié Nishikawa, Shuh-ichi Yamamoto, Hayashi Endo, Toshiya
author_sort	Tamura, Yasushi
title	Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
title_short	Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
title_full	Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
title_fullStr	Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
title_full_unstemmed	Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria
title_sort	identification of tam41 maintaining integrity of the tim23 protein translocator complex in mitochondria
description	Newly synthesized mitochondrial proteins are imported into mitochondria with the aid of protein translocator complexes in the outer and inner mitochondrial membranes. We report the identification of yeast Tam41, a new member of mitochondrial protein translocator systems. Tam41 is a peripheral inner mitochondrial membrane protein facing the matrix. Disruption of the TAM41 gene led to temperature-sensitive growth of yeast cells and resulted in defects in protein import via the TIM23 translocator complex at elevated temperature both in vivo and in vitro. Although Tam41 is not a constituent of the TIM23 complex, depletion of Tam41 led to a decreased molecular size of the TIM23 complex and partial aggregation of Pam18 and -16. Import of Pam16 into mitochondria without Tam41 was retarded, and the imported Pam16 formed aggregates in vitro. These results suggest that Tam41 facilitates mitochondrial protein import by maintaining the functional integrity of the TIM23 protein translocator complex from the matrix side of the inner membrane.
publisher	The Rockefeller University Press
publishDate	2006
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2064306/
_version_	1611406554476576768

Identification of Tam41 maintaining integrity of the TIM23 protein translocator complex in mitochondria

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