Membrane protein insertion and assembly by the bacterial holo-translocon SecYEG-SecDF-YajC-YidC
Autor(en): | Komar, Joanna Alvira, Sara Schulze, Ryan J. Martin, Remy Nijeholt, Jelger A. Lycklama A. Lee, Sarah C. Dafforn, Tim R. Deckers-Hebestreit, Gabriele Berger, Imre Schaffitzel, Christiane Collinson, Ian |
Stichwörter: | Biochemistry & Molecular Biology; CONDUCTING CHANNEL; CYTOPLASMIC MEMBRANE; ESCHERICHIA-COLI YIDC; F1F0 ATP SYNTHASE; INNER MEMBRANE; NASCENT FTSQ; PROJECTION STRUCTURE; SIGNAL RECOGNITION PARTICLE; SYNTHASE SUBUNIT-C; TRANSLATING RIBOSOME | Erscheinungsdatum: | 2016 | Herausgeber: | PORTLAND PRESS LTD | Journal: | BIOCHEMICAL JOURNAL | Volumen: | 473 | Ausgabe: | 19 | Startseite: | 3341 | Seitenende: | 3354 | Zusammenfassung: | Protein secretion and membrane insertion occur through the ubiquitous Sec machinery. In this system, insertion involves the targeting of translating ribosomes via the signal recognition particle and its cognate receptor to the SecY (bacteria and archaea)/Sec61 (eukaryotes) translocon. A common mechanism then guides nascent transmembrane helices (TMHs) through the Sec complex, mediated by associated membrane insertion factors. In bacteria, the membrane protein `insertase' YidC ushers TMHs through a lateral gate of SecY to the bilayer. YidC is also thought to incorporate proteins into the membrane independently of SecYEG. Here, we show the bacterial holo-translocon (HTL) a supercomplex of SecYEG-SecDF-YajC-YidC - is a bona fide resident of the Escherichia coli inner membrane. Moreover, when compared with SecYEG and YidC alone, the HTL is more effective at the insertion and assembly of a wide range of membrane protein substrates, including those hitherto thought to require only YidC. |
ISSN: | 02646021 | DOI: | 10.1042/BCJ20160545 |
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geprüft am 01.06.2024