Open AccessStructural insight into the SAM-mediated assembly of the mitochondrial TOM core complex
Author(s) -
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
Publication year - 2021
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.abh0704
Subject(s) - translocase , biogenesis , barrel (horology) , protein subunit , translocase of the outer membrane , organelle , microbiology and biotechnology , biology , protein targeting , inner mitochondrial membrane , molecular machine , bacterial outer membrane , mitochondrion , membrane protein , chemistry , membrane , mitochondrial membrane transport protein , biochemistry , genetics , gene , escherichia coli , chromosomal translocation , materials science , composite material
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. Wanget 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
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