Dissecting the twin-arginine translocation pathway using genome-wide analysis

被引:9
作者
Bronstein, P
Marrichi, M
DeLisa, MP [1 ]
机构
[1] Cornell Univ, Sch Chem & Biomol Engn, Ithaca, NY 14853 USA
[2] Cornell Univ, Dept Plant Pathol, Ithaca, NY 14853 USA
[3] Cornell Univ, Dept Biomed Engn, Ithaca, NY 14853 USA
关键词
twin-arginine translocation; protein export;
D O I
10.1016/j.resmic.2004.06.013
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
A recently discovered route for protein export, known as the twin-arginine translocation (Tat) pathway, has received much attention owing to several atypical characteristics that distinguish it from other transport mechanisms. For instance, recent evidence has clearly established that this pathway only transports folded polypeptides. Moreover, several studies have demonstrated a vital role for the Tat pathway in bacterial pathogenesis. In this review, we discuss genomic approaches that have been employed to determine the prevalence and capacity of the Tat system and how the information generated from these approaches is helping to connect Tat transport to bacterial physiology and virulence. (C) 2004 Elsevier SAS. All rights reserved.
引用
收藏
页码:803 / 810
页数:8
相关论文
共 76 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]   Energetics of protein transport across biological membranes:: A study of the thylakoid ΔpH-dependent/cpTat pathway [J].
Alder, NN ;
Theg, SM .
CELL, 2003, 112 (02) :231-242
[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 novel protein transport system involved in the biogenesis of bacterial electron transfer chains [J].
Berks, BC ;
Sargent, F ;
De Leeuw, E ;
Hinsley, AP ;
Stanley, NR ;
Jack, RL ;
Buchanan, G ;
Palmer, T .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2000, 1459 (2-3) :325-330
[6]   A common export pathway for proteins binding complex redox cofactors? [J].
Berks, BC .
MOLECULAR MICROBIOLOGY, 1996, 22 (03) :393-404
[7]   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
[8]   Protein secretion by Gram-negative bacterial ABC exporters - A review [J].
Binet, R ;
Letoffe, S ;
Ghigo, JM ;
Delepelaire, P ;
Wandersman, C .
GENE, 1997, 192 (01) :7-11
[9]   Genetic analysis of pathway specificity during posttranslational protein translocation across the Escherichia coli plasma membrane [J].
Blaudeck, N ;
Kreutzenbeck, P ;
Freudl, R ;
Sprenger, GA .
JOURNAL OF BACTERIOLOGY, 2003, 185 (09) :2811-2819
[10]   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