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

被引:179
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
[1]   Differential interactions between a twin-arginine signal peptide and its translocase in Escherichia coli [J].
Alami, M ;
Lüke, I ;
Deitermann, S ;
Eisner, G ;
Koch, HG ;
Brunner, J ;
Müller, M .
MOLECULAR CELL, 2003, 12 (04) :937-946
[2]   Cell biology - Shape-shifting protein channel [J].
Benach, J ;
Hunt, JF .
NATURE, 2004, 427 (6969) :24-26
[3]   The Tat protein export pathway [J].
Berks, BC ;
Sargent, F ;
Palmer, T .
MOLECULAR MICROBIOLOGY, 2000, 35 (02) :260-274
[4]   The Tat protein translocation pathway and its role in microbial physiology [J].
Berks, BC ;
Palmer, T ;
Sargent, F .
ADVANCES IN MICROBIAL PHYSIOLOGY, VOL 47, 2003, 47 :187-254
[5]   A common export pathway for proteins binding complex redox cofactors? [J].
Berks, BC .
MOLECULAR MICROBIOLOGY, 1996, 22 (03) :393-404
[6]   The Escherichia coli amidase AmiC is a periplasmic septal ring component exported via the twin-arginine transport pathway [J].
Bernhardt, TG ;
de Boer, PAJ .
MOLECULAR MICROBIOLOGY, 2003, 48 (05) :1171-1182
[7]   Isolation and characterization of bifunctional Escherichia coli TatA mutant proteins that allow efficient Tat-dependent protein translocation in the absence of TatB [J].
Blaudeck, N ;
Kreutzenbeck, P ;
Müller, M ;
Sprenger, GA ;
Freudl, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (05) :3426-3432
[8]   An essential component of a novel bacterial protein export system with homologues in plastids and mitochondria [J].
Bogsch, EG ;
Sargent, F ;
Stanley, NR ;
Berks, BC ;
Robinson, C ;
Palmer, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (29) :18003-18006
[9]   Protein transport in the halophilic archaeon ARTICLE Halobacterium sp NRC-1:: a major role for the twin-arginine translocation pathway? [J].
Bolhuis, A .
MICROBIOLOGY-SGM, 2002, 148 :3335-3346
[10]   TatB and TatC form a functional and structural unit of the twin-arginine translocase from Escherichia coli [J].
Bolhuis, A ;
Mathers, JE ;
Thomas, JD ;
Barrett, CML ;
Robinson, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (23) :20213-20219