Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex

Author:

Wang Qiang1ORCID,Guan Zeyuan1ORCID,Qi Liangbo1ORCID,Zhuang Jinjin1ORCID,Wang Chen1ORCID,Hong Sixing1ORCID,Yan Ling1ORCID,Wu Yan1ORCID,Cao Xiaoqian1,Cao Jianbo2ORCID,Yan Junjie1ORCID,Zou Tingting3ORCID,Liu Zhu1ORCID,Zhang Delin1ORCID,Yan Chuangye4ORCID,Yin Ping1ORCID

Affiliation:

1. National Key Laboratory of Crop Genetic Improvement, Hubei Hongshan Laboratory, Huazhong Agricultural University, Wuhan 430070, China.

2. Public Laboratory of Electron Microscopy, Huazhong Agricultural University, Wuhan 430070, China.

3. College of Life Science and Technology, Huazhong Agricultural University, Wuhan 430070, China.

4. Beijing Advanced Innovation Center for Structural Biology, Tsinghua-Peking Joint Center for Life Sciences, School of Life Sciences, Tsinghua University, Beijing 100084, China.

Abstract

Barrels that build barrels Cells produce specialized machinery to produce functional β-barrel proteins that are involved in cross-membrane transport and membrane protein biogenesis in eukaryotic organelles and some bacteria. Wang et al . studied one of these systems that is itself a β-barrel, the mitochondrial sorting and assembly machinery (SAM), in complex with one of its client proteins, translocase of the outer membrane (TOM). TOM subunits can be added one at a time while the protein is bound to SAM. Compared with the full TOM core complex, the final TOM core subunit clashes with SAM and suggests that release of TOM may be driven by its association. —MAF

Funder

National Natural Science Foundation of China

China Postdoctoral Science Foundation

Ministry of Science and Technology of China

the Fundamental Research Funds for the Central Universities

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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