Protein targeting by the bacterial twin-arginine translocation (Tat) pathway

被引:181
作者
Berks, BC
Palmer, T
Sargent, F
机构
[1] Univ Oxford, Dept Biochem, Oxford OX1 3QU, England
[2] John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England
[3] Univ E Anglia, Sch Biol Sci, Norwich NR4 7TJ, Norfolk, England
基金
英国医学研究理事会;
关键词
D O I
10.1016/j.mib.2005.02.010
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
The Tat (twin-arginine translocation) protein export system is found in the cytoplasmic membrane of most prokaryotes; and is dedicated to the transport of folded proteins. The Tat system is now known to be essential for many bacterial processes including energy metabolism, cell wall biosynthesis, the nitrogen-fixing symbiosis and bacterial pathogenesis. Recent studies demonstrate that substrate-specific accessory proteins prevent improperly assembled substrates from interacting with the Tat transporter. During the transport cycle itself substrate proteins bind to a receptor complex in the membrane which then recruits a protein-translocating channel to carry out the transport reaction.
引用
收藏
页码:174 / 181
页数:8
相关论文
共 53 条
[41]   Contribution of the twin arginine translocation system to the virulence of enterohemorrhagic Escherichia coli O157:H7 [J].
Pradel, N ;
Ye, CY ;
Livrelli, V ;
Xu, HG ;
Joly, B ;
Wu, LF .
INFECTION AND IMMUNITY, 2003, 71 (09) :4908-4916
[42]   Adaptation of protein secretion to extremely high-salt conditions by extensive use of the twin-arginine translocation pathway [J].
Rose, RW ;
Brüser, T ;
Kissinger, JC ;
Pohlschröder, M .
MOLECULAR MICROBIOLOGY, 2002, 45 (04) :943-950
[43]   An Escherichia coli twin-arginine signal peptide switches between helical and unstructured conformations depending on the hydrophobicity of the environment [J].
San Miguel, M ;
Marrington, R ;
Rodger, PM ;
Rodger, A ;
Robinson, C .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2003, 270 (16) :3345-3352
[44]   Purified components of the Escherichia coli Tat protein transport system form a double-layered ring structure [J].
Sargent, F ;
Gohlke, U ;
de Leeuw, E ;
Stanley, NR ;
Palmer, T ;
Saibil, HR ;
Berks, BC .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 2001, 268 (12) :3361-3367
[45]   Overlapping functions of components of a bacterial Sec-independent protein export pathway [J].
Sargent, F ;
Bogsch, EG ;
Stanley, NR ;
Wexler, M ;
Robinson, C ;
Berks, BC ;
Palmer, T .
EMBO JOURNAL, 1998, 17 (13) :3640-3650
[46]   Sec-independent protein translocation in Escherichia coli -: A distinct and pivotal role for the TatB protein [J].
Sargent, F ;
Stanley, NR ;
Berks, BC ;
Palmer, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (51) :36073-36082
[47]   Escherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope [J].
Stanley, NR ;
Findlay, K ;
Berks, BC ;
Palmer, T .
JOURNAL OF BACTERIOLOGY, 2001, 183 (01) :139-144
[48]   The thylakoid ΔpH-dependent pathway machinery facilitates RR-independent N-tail protein integration [J].
Summer, EJ ;
Mori, H ;
Settles, AM ;
Cline, K .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2000, 275 (31) :23483-23490
[49]   Sequence analysis of bacterial redox enzyme maturation proteins (REMPs) [J].
Turner, RJ ;
Papish, AL ;
Sargent, F .
CANADIAN JOURNAL OF MICROBIOLOGY, 2004, 50 (04) :225-238
[50]   Involvement of the twin-arginine translocation system in protein secretion via the type II pathway [J].
Voulhoux, R ;
Ball, G ;
Ize, B ;
Vasil, ML ;
Lazdunski, A ;
Wu, LF ;
Filloux, A .
EMBO JOURNAL, 2001, 20 (23) :6735-6741