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- W1979093610 abstract "Many proteins are translocated across, or integrated into, membranes. Both functions are fulfilled by the 'translocon/translocase', which contains a membrane-embedded protein-conducting channel (PCC) and associated soluble factors that drive translocation and insertion reactions using nucleotide triphosphates as fuel. This perspective focuses on reinterpreting existing experimental data in light of a recently proposed PCC model comprising a front-to-front dimer of SecY or Sec61 heterotrimeric complexes. In this new framework, we propose (i) a revised model for SRP-SR–mediated docking of the ribosome–nascent polypeptide to the PCC; (ii) that the dynamic interplay between protein substrate, soluble factors and PCC controls the opening and closing of a transmembrane channel across, and/or a lateral gate into, the membrane; and (iii) that co- and post-translational translocation, involving the ribosome and SecA, respectively, not only converge at the PCC but also use analogous mechanisms for coordinating protein translocation." @default.
- W1979093610 created "2016-06-24" @default.
- W1979093610 creator A5018058661 @default.
- W1979093610 creator A5042892654 @default.
- W1979093610 creator A5068549255 @default.
- W1979093610 date "2006-11-01" @default.
- W1979093610 modified "2023-09-27" @default.
- W1979093610 title "Co- and post-translational translocation through the protein-conducting channel: analogous mechanisms at work?" @default.
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- W1979093610 doi "https://doi.org/10.1038/nsmb1166" @default.
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