Publication

SecA, a remarkable nanomachine

Kusters, I. & Driessen, A. J. M., Jun-2011, In : Cellular and molecular life sciences. 68, 12, p. 2053-2066 14 p.

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DOI

Biological cells harbor a variety of molecular machines that carry out mechanical work at the nanoscale. One of these nanomachines is the bacterial motor protein SecA which translocates secretory proteins through the protein-conducting membrane channel SecYEG. SecA converts chemically stored energy in the form of ATP into a mechanical force to drive polypeptide transport through SecYEG and across the cytoplasmic membrane. In order to accommodate a translocating polypeptide chain and to release transmembrane segments of membrane proteins into the lipid bilayer, SecYEG needs to open its central channel and the lateral gate. Recent crystal structures provide a detailed insight into the rearrangements required for channel opening. Here, we review our current understanding of the mode of operation of the SecA motor protein in concert with the dynamic SecYEG channel. We conclude with a new model for SecA-mediated protein translocation that unifies previous conflicting data.

Original languageEnglish
Pages (from-to)2053-2066
Number of pages14
JournalCellular and molecular life sciences
Volume68
Issue number12
Publication statusPublished - Jun-2011

    Keywords

  • SecA, SecYEG, Protein translocation, ESCHERICHIA-COLI SECA, PROTEIN-TRANSLOCATION CHANNEL, SIGNAL-SEQUENCE RECOGNITION, DISTINCT ATP-BINDING, X-RAY-STRUCTURE, PREPROTEIN TRANSLOCATION, IN-VIVO, CONDUCTING CHANNEL, DIMERIC SECA, RIBOSOME-BINDING

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