The Tat protein export pathway

被引：461

作者：

Berks, BC ^{[1
]}

Sargent, F

Palmer, T

机构：

[1] Univ E Anglia, Sch Biol Sci, Ctr Met Prot Spect & Biol, Norwich NR4 7TJ, Norfolk, England

[2] John Innes Ctr Plant Sci Res, Dept Mol Microbiol, Norwich NR4 7UH, Norfolk, England

来源：

MOLECULAR MICROBIOLOGY | 2000年 / 35卷 / 02期

关键词：

D O I：

10.1046/j.1365-2958.2000.01719.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 [生物化学与分子生物学]; 081704 [应用化学];

摘要：

The Tat (twin-arginine translocation) system is a bacterial protein export pathway with the remarkable ability to transport folded proteins across the cytoplasmic membrane. Preproteins are directed to the Tat pathway by signal peptides that bear a characteristic sequence motif, which includes consecutive arginine residues. Here, we review recent progress on the characterization of the Tat system and critically discuss the structure and operation of this major new bacterial protein export pathway.

引用

页码：260 / 274

页数：15

共 93 条

[1]

Topological analysis of the aerobic membrane-bound formate dehydrogenase of Escherichia coli [J].

Benoit, S ;

Abaibou, H ;

Mandrand-Berthelot, MA .

JOURNAL OF BACTERIOLOGY, 1998, 180 (24) :6625-6634

[2]

Structural and dynamical properties of a partially unfolded Fe4S4 protein:: Role of the cofactor in protein folding [J].

Bentrop, D ;

Bertini, I ;

Iacoviello, R ;

Luchinat, C ;

Niikura, Y ;

Piccioli, M ;

Presenti, C ;

Rosato, A .

BIOCHEMISTRY, 1999, 38 (15) :4669-4680

[3]

BERG BL, 1991, J BIOL CHEM, V266, P22380

[4]

A common export pathway for proteins binding complex redox cofactors? [J].

Berks, BC .

MOLECULAR MICROBIOLOGY, 1996, 22 (03) :393-404

[5]

The Alcaligenes eutrophus membrane-bound hydrogenase gene locus encodes functions involved in maturation and electron transport coupling [J].

Bernhard, M ;

Schwartz, E ;

Rietdorf, J ;

Friedrich, B .

JOURNAL OF BACTERIOLOGY, 1996, 178 (15) :4522-4529

[6]

Pathway specificity for a Delta pH-dependent precursor thylakoid lumen protein is governed by a 'Sec-avoidance' motif in the transfer peptide and a 'Sec-incompatible' mature protein [J].

Bogsch, E ;

Brink, S ;

Robinson, C .

EMBO JOURNAL, 1997, 16 (13) :3851-3859

[7]

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

[8]

Brüser T, 1998, FEMS MICROBIOL LETT, V164, P329

[9]

CARTER CW, 1974, J BIOL CHEM, V249, P4214

[10]

A NEW-TYPE OF SIGNAL PEPTIDE - CENTRAL ROLE OF A TWIN-ARGININE MOTIF IN TRANSFER SIGNALS FOR THE DELTA-PH-DEPENDENT THYLAKOIDAL PROTEIN TRANSLOCASE [J].

CHADDOCK, AM ;

MANT, A ;

KARNAUCHOV, I ;

BRINK, S ;

HERRMANN, RG ;

KLOSGEN, RB ;

ROBINSON, C .

EMBO JOURNAL, 1995, 14 (12) :2715-2722

← 1 2 3 4 5 6 7 8 9 10 →