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

信息来源:     发布时间:2021-09-01

QIANG WANG HTTPS://ORCID.ORG/0000-0002-7048-638XZEYUAN GUAN HTTPS://ORCID.ORG/0000-0002-8909-866XLIANGBO QI HTTPS://ORCID.ORG/0000-0003-2867-0009JINJIN ZHUANG HTTPS://ORCID.ORG/0000-0003-2058-5213CHEN WANG HTTPS://ORCID.ORG/0000-0002-0508-0084SIXING HONG HTTPS://ORCID.ORG/0000-0002-0210-5645LING YAN HTTPS://ORCID.ORG/0000-0002-1437-2193YAN WU HTTPS://ORCID.ORG/0000-0001-7814-3923XIAOQIAN CAOJIANBO CAO HTTPS://ORCID.ORG/0000-0003-3738-5082JUNJIE YAN HTTPS://ORCID.ORG/0000-0001-9748-7246TINGTING ZOU HTTPS://ORCID.ORG/0000-0002-7240-1378ZHU LIU HTTPS://ORCID.ORG/0000-0003-4073-7237DELIN ZHANG HTTPS://ORCID.ORG/0000-0002-5299-0718CHUANGYE YAN HTTPS://ORCID.ORG/0000-0001-9338-8048AND PING YIN HTTPS://ORCID.ORG/0000-0001-8001-221X


SCIENCE26 Aug 2021Preprint

DOI: 10.1126/science.abh0704









HTTPS://ORCID.ORG/0000-0001-8001-

Abstract

β-barrel outer membrane proteins (β-OMPs) play vital roles in mitochondria, chloroplasts, and Gram-negative bacteria. Evolutionarily conserved complexes such as the mitochondrial sorting and assembly machinery (SAM) mediate the assembly of β-OMPs. Here, we investigated the SAM-mediated assembly of the translocase of the outer membrane (TOM) core complex. Cryo-electron microscopy structures of SAM-fully folded Tom40 and the SAM-Tom40/Tom5/Tom6 complexes at ~3-Å resolution reveal that Sam37 stabilizes the mature Tom40 mainly through electrostatic interactions, thus facilitating subsequent TOM assembly. These results support the β-barrel switching model and provide structural insights into the assembly and release of β-barrel complexes.


全文链接:https://www.science.org/doi/full/10.1126/science.abh0704

 


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