Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane—Distinct translocases and mechanisms |
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Authors: | Paolo Natale Thomas Brüser |
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Institution: | a Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute and the Zernike Institute for Advanced Materials, University of Groningen, Kerklaan 30, 9751 NN HAREN, The Netherlands b Institute of Biology, Department of Microbiology, University of Halle, Kurt-Mothes-Str. 3, 06120 Halle, Germany |
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Abstract: | In bacteria, two major pathways exist to secrete proteins across the cytoplasmic membrane. The general Secretion route, termed Sec-pathway, catalyzes the transmembrane translocation of proteins in their unfolded conformation, whereupon they fold into their native structure at the trans-side of the membrane. The Twin-arginine translocation pathway, termed Tat-pathway, catalyses the translocation of secretory proteins in their folded state. Although the targeting signals that direct secretory proteins to these pathways show a high degree of similarity, the translocation mechanisms and translocases involved are vastly different. |
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Keywords: | Secretion SecA SecY Twin arginine Tat |
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