Abstract
Secretion of most polypeptides across the bacterial plasma membrane is catalyzed by the Sec protein translocase. This complex molecular machine comprises a flexible transmembrane conduit coupled to a motor‐like component and displays four activities: (a) it is a specific receptor at its cytoplasmic side for all secretory polypeptides, (b) it converts metabolic energy from ATP and proton gradients into mechanical motion, (c) it prevents substrates from folding in statu translocanti and (d) it binds and releases short segments of the polymeric substrate sequentially. Combination of these activities allows translocase to move processively along the length of the substrate. Substrates are thus gradually expelled from the membrane and are released for subsequent extracytoplasmic folding.
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Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 25, 2002, 12:02 p.m.) |
Deposited | 1 year, 11 months ago (Sept. 16, 2023, 1:47 p.m.) |
Indexed | 5 months, 2 weeks ago (March 19, 2025, 11:23 a.m.) |
Issued | 25 years, 2 months ago (June 26, 2000) |
Published | 25 years, 2 months ago (June 26, 2000) |
Published Online | 25 years, 2 months ago (June 26, 2000) |
Published Print | 25 years, 2 months ago (June 30, 2000) |
@article{Economou_2000, title={Bacterial protein translocase: a unique molecular machine with an army of substrates}, volume={476}, ISSN={1873-3468}, url={http://dx.doi.org/10.1016/s0014-5793(00)01662-8}, DOI={10.1016/s0014-5793(00)01662-8}, number={1–2}, journal={FEBS Letters}, publisher={Wiley}, author={Economou, Anastassios}, year={2000}, month=jun, pages={18–21} }