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

2021; American Association for the Advancement of Science; Volume: 373; Issue: 6561 Linguagem: Inglês

10.1126/science.abh0704

1095-9203

Qiang Wang, Zeyuan Guan, Liangbo Qi, Jinjin Zhuang, Chen Wang, Sixing Hong, Ling Yan, Yan Wu, Xiaoqian Cao, Jianbo Cao, Junjie Yan, Tingting Zou, Zhu Liu, Delin Zhang, Chuangye Yan, Ping Yin,

ATP Synthase and ATPases Research

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