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Co- and post-translational translocation through the protein-conducting channel: Analogous mechanisms at work?

Nature Structural and Molecular Biology, ISSN: 1545-9993, Vol: 13, Issue: 11, Page: 957-964
2006
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Review Description

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. © 2006 Nature Publishing Group.

Bibliographic Details

Mitra, Kakoli; Frank, Joachim; Driessen, Arnold

Springer Science and Business Media LLC

Biochemistry, Genetics and Molecular Biology

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