Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex
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. 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-angstrom 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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2021 |
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| Erschienen: |
2021 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:373 |
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| Enthalten in: |
Science (New York, N.Y.) - 373(2021), 6561 vom: 17. Sept., Seite 1377-1381 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Wang, Qiang [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 24.09.2021 Date Revised 02.03.2022 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1126/science.abh0704 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM329893513 |
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| 245 | 1 | 0 | |a Structural insight into the SAM-mediated assembly of the mitochondrial TOM core complex |
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| 520 | |a 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. 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-angstrom 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 7 | |a Carrier Proteins |2 NLM | |
| 650 | 7 | |a Membrane Proteins |2 NLM | |
| 650 | 7 | |a Mitochondrial Membrane Transport Proteins |2 NLM | |
| 650 | 7 | |a Mitochondrial Precursor Protein Import Complex Proteins |2 NLM | |
| 650 | 7 | |a Multiprotein Complexes |2 NLM | |
| 650 | 7 | |a Protein Subunits |2 NLM | |
| 650 | 7 | |a SAM37 protein, S cerevisiae |2 NLM | |
| 650 | 7 | |a Saccharomyces cerevisiae Proteins |2 NLM | |
| 650 | 7 | |a Tom40 protein, S cerevisiae |2 NLM | |
| 700 | 1 | |a Guan, Zeyuan |e verfasserin |4 aut | |
| 700 | 1 | |a Qi, Liangbo |e verfasserin |4 aut | |
| 700 | 1 | |a Zhuang, Jinjin |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Chen |e verfasserin |4 aut | |
| 700 | 1 | |a Hong, Sixing |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Ling |e verfasserin |4 aut | |
| 700 | 1 | |a Wu, Yan |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Xiaoqian |e verfasserin |4 aut | |
| 700 | 1 | |a Cao, Jianbo |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Junjie |e verfasserin |4 aut | |
| 700 | 1 | |a Zou, Tingting |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Zhu |e verfasserin |4 aut | |
| 700 | 1 | |a Zhang, Delin |e verfasserin |4 aut | |
| 700 | 1 | |a Yan, Chuangye |e verfasserin |4 aut | |
| 700 | 1 | |a Yin, Ping |e verfasserin |4 aut | |
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