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Molecular architecture of the active mitochondrial protein gate
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Number of Authors: 17
2015 (English)In: Science, ISSN 0036-8075, E-ISSN 1095-9203, Vol. 349, no 6255, 1544-1548 p.Article in journal (Refereed) Published
Abstract [en]

Mitochondria fulfill central functions in cellular energetics, metabolism, and signaling. The outer membrane translocator complex (the TOM complex) imports most mitochondrial proteins, but its architecture is unknown. Using a cross-linking approach, we mapped the active translocator down to single amino acid residues, revealing different transport paths for preproteins through the Tom40 channel. An N-terminal segment of Tom40 passes from the cytosol through the channel to recruit chaperones fromthe intermembrane space that guide the transfer of hydrophobic preproteins. The translocator contains three Tom40 beta-barrel channels sandwiched between a central alpha-helical Tom22 receptor cluster and external regulatory Tom proteins. The preprotein-translocating trimeric complex exchanges with a dimeric isoform to assemble new TOM complexes. Dynamic coupling of alpha-helical receptors, beta-barrel channels, and chaperones generates a versatile machinery that transports about 1000 different proteins.

Place, publisher, year, edition, pages
2015. Vol. 349, no 6255, 1544-1548 p.
National Category
Biological Sciences Medical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)
URN: urn:nbn:se:su:diva-121872DOI: 10.1126/science.aac6428ISI: 000361707000049PubMedID: 26404837OAI: diva2:862672
Swedish Research Council
Available from: 2015-10-23 Created: 2015-10-19 Last updated: 2016-02-19Bibliographically approved

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Elofsson, Arne
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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Biological SciencesMedical Biotechnology (with a focus on Cell Biology (including Stem Cell Biology), Molecular Biology, Microbiology, Biochemistry or Biopharmacy)

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