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TitleAn ER translocon for multi-pass membrane protein biogenesis.
Journal, issue, pagesElife, Vol. 9, Year 2020
Publish dateAug 21, 2020
AuthorsPhilip T McGilvray / S Andrei Anghel / Arunkumar Sundaram / Frank Zhong / Michael J Trnka / James R Fuller / Hong Hu / Alma L Burlingame / Robert J Keenan /
PubMed AbstractMembrane proteins with multiple transmembrane domains play critical roles in cell physiology, but little is known about the machinery coordinating their biogenesis at the endoplasmic reticulum. Here ...Membrane proteins with multiple transmembrane domains play critical roles in cell physiology, but little is known about the machinery coordinating their biogenesis at the endoplasmic reticulum. Here we describe a ~ 360 kDa ribosome-associated complex comprising the core Sec61 channel and five accessory factors: TMCO1, CCDC47 and the Nicalin-TMEM147-NOMO complex. Cryo-electron microscopy reveals a large assembly at the ribosome exit tunnel organized around a central membrane cavity. Similar to protein-conducting channels that facilitate movement of transmembrane segments, cytosolic and luminal funnels in TMCO1 and TMEM147, respectively, suggest routes into the central membrane cavity. High-throughput mRNA sequencing shows selective translocon engagement with hundreds of different multi-pass membrane proteins. Consistent with a role in multi-pass membrane protein biogenesis, cells lacking different accessory components show reduced levels of one such client, the glutamate transporter EAAT1. These results identify a new human translocon and provide a molecular framework for understanding its role in multi-pass membrane protein biogenesis.
External linksElife / PubMed:32820719 / PubMed Central
MethodsEM (single particle)
Resolution3.4 - 3.84 Å
Structure data

EMDB-21426:
Single Particle Cryo-EM Structure of the Natively Isolated Sec61 complex, TMCO1, Nicalin, TMEM147, and CCDC47 Containing Translocon
Method: EM (single particle) / Resolution: 3.84 Å

EMDB-21427:
Single Particle Cryo-EM Structure of the Natively Isolated Sec61, TMCO1, Nicalin, TMEM147, and CCDC47 Containing Ribosome-Translocon Complex
Method: EM (single particle) / Resolution: 3.4 Å

21435

6w6l

EMDB-21435: Single Particle Cryo-EM Structure of the Natively Isolated Sec61, TMCO1, Nicalin, TMEM147, and CCDC47 Containing Ribosome-Translocon Complex After Focused Refinement with Local Angular Searches
PDB-6w6l: Cryo-EM structure of the human ribosome-TMCO1 translocon
Method: EM (single particle) / Resolution: 3.8 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

Source
  • homo sapiens (human)
KeywordsRIBOSOME/PROTEIN TRANSPORT / RIBOSOME-PROTEIN TRANSPORT complex

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