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Sec- and Tat-mediated protein secretion across the bacterial cytoplasmic membrane -: Distinct translocases and mechanisms
被引:372
作者:
Natale, Paolo
[1
,2
]
Brueser, Thomas
[3
]
Driessen, Arnold J. M.
[1
,2
]
机构:
[1] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Dept Microbiol, NL-9751 NN Haren, Netherlands
[2] Univ Groningen, Zernike Inst Adv Mat, NL-9751 NN Haren, Netherlands
[3] Univ Halle Wittenberg, Dept Microbiol, Inst Biol, D-06120 Halle, Germany
来源:
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
|
2008年
/
1778卷
/
09期
关键词:
secretion;
SecA;
SecY;
twin arginine;
Tat;
D O I:
10.1016/j.bbamem.2007.07.015
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
In bacteria, two major pathways exist to secrete proteins across the cytoplasmic membrane. The general Secretion route, termed Sec-pathway, catalyzes the transmembrame 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. (C) 2007 Elsevier B.V. All rights reserved.
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页码:1735 / 1756
页数:22
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