Bacterial protein secretion through the translocase nanomachine

被引:188
作者
Papanikou, Effrosyni
Karamanou, Spyridoula
Economou, Anastassios
机构
[1] Fdn Res & Technol Hellas, Inst Mol Biol & Biotechnol, GR-71110 Iraklion, Greece
[2] Univ Crete, Dept Biol, GR-71110 Iraklion, Greece
关键词
D O I
10.1038/nrmicro1771
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
All cells must traffic proteins across their membranes. This essential process is responsible for the biogenesis of membranes and cell walls, motility and nutrient scavenging and uptake, and is also involved in pathogenesis and symbiosis. The translocase is an impressively dynamic nanomachine that is the central component which catalyses transmembrane crossing. This complex, multi-stage reaction involves a cascade of inter- and intramolecular interactions that select, sort and target polypeptides to the membrane, and use energy to promote the movement of these polypeptides across - or their lateral escape and integration into - the phospholipid bilayer, with high fidelity and efficiency. Here, we review the most recent data on the structure and function of the translocase nanomachine.
引用
收藏
页码:839 / 851
页数:13
相关论文
共 134 条
[41]   Nucleotide exchange from the high-affinity ATP-binding site in SecA is the rate-limiting step in the ATPase cycle of the soluble enzyme and occurs through a specialized conformational state [J].
Fak, JJ ;
Itkin, A ;
Ciobanu, DD ;
Lin, EC ;
Song, XJ ;
Chou, YT ;
Gierasch, LM ;
Hunt, JF .
BIOCHEMISTRY, 2004, 43 (23) :7307-7327
[42]   Zinc stabilizes the SecB binding site of SecA [J].
Fekkes, P ;
de Wit, JG ;
Boorsma, A ;
Friesen, RHE ;
Driessen, AJM .
BIOCHEMISTRY, 1999, 38 (16) :5111-5116
[43]   The molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation [J].
Fekkes, P ;
vanderDoes, C ;
Driessen, AJM .
EMBO JOURNAL, 1997, 16 (20) :6105-6113
[44]   INITIAL STEPS IN PROTEIN MEMBRANE INSERTION - BACTERIOPHAGE-M13 PROCOAT PROTEIN BINDS TO THE MEMBRANE-SURFACE BY ELECTROSTATIC INTERACTION [J].
GALLUSSER, A ;
KUHN, A .
EMBO JOURNAL, 1990, 9 (09) :2723-2729
[45]   Protein disulfide isomerase: the structure of oxidative folding [J].
Gruber, Christian W. ;
Cemazar, Maga ;
Heras, Begona ;
Martin, Jennifer L. ;
Craik, David J. .
TRENDS IN BIOCHEMICAL SCIENCES, 2006, 31 (08) :455-464
[46]   Molecular dynamics studies of the archaeal translocon [J].
Gumbart, J ;
Schulten, K .
BIOPHYSICAL JOURNAL, 2006, 90 (07) :2356-2367
[47]   The aqueous pore through the translocon has a diameter of 40-60 angstrom during cotranslational protein translocation at the ER membrane [J].
Hamman, BD ;
Chen, JC ;
Johnson, EE ;
Johnson, AE .
CELL, 1997, 89 (04) :535-544
[48]   Oligomeric rings of the Sec61p complex induced by ligands required for protein translocation [J].
Hanein, D ;
Matlack, KES ;
Jungnickel, B ;
Plath, K ;
Kalies, KU ;
Miller, KR ;
Rapoport, TA ;
Akey, CW .
CELL, 1996, 87 (04) :721-732
[49]   THE BINDING CASCADE OF SECB TO SECA TO SECY/E MEDIATES PREPROTEIN TARGETING TO THE ESCHERICHIA-COLI PLASMA-MEMBRANE [J].
HARTL, FU ;
LECKER, S ;
SCHIEBEL, E ;
HENDRICK, JP ;
WICKNER, W .
CELL, 1990, 63 (02) :269-279
[50]   The carboxyl-terminal region is essential for Sec-A dimerization [J].
Hirano, M ;
Matsuyama, S ;
Tokuda, H .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1996, 229 (01) :90-95