Title: Bacterial protein translocase: a unique molecular machine with an army of substrates
Authors: Economou, Anastassios # ×
Issue Date: Jun-2000
Publisher: Elsevier on behalf of the Federation of European Biochemical Societies
Series Title: FEBS Letters vol:476 issue:1-2 pages:18-21
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.
ISSN: 0014-5793
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Non-KU Leuven Association publications
× corresponding author
# (joint) last author

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