The underlying mechanisms of type II protein secretion

被引:217
作者
Filloux, A [1 ]
机构
[1] CNRS, IBSM, UPR9027, Lab Ingn Syst Macromol, F-13402 Marseille 20, France
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH | 2004年 / 1694卷 / 1-3期
关键词
type IV pilus; general secretory pathway or GSP; secretin; pseudopilin and pseudopilus; traffic ATPase; gram-negative bacteria;
D O I
10.1016/j.bbamcr.2004.05.003
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The cell envelope of Gram-negative bacteria is composed of two membranes. which are separated by the peptidoglycan-containing periplasm. Whereas the envelope forms all essential barrier against harmful substances, it is nevertheless a compartment of intense traffic for large proteins such as enzymes and toxins. Numerous studies dealing with the molecular mechanism of protein secretion have revealed that Gram-negative bacteria evolved different strategies to achieve this process. Among them, the type II secretion mechanism is pm of a two-step process. Exoproteins following this pathway are synthesized as signal peptide-containing precursors. After cleavage of the signal peptide, the mature exoproteins are released into the periplasm, where they fold. The type II machinery, also known as the secreton, is responsible for the translocation of the periplasmic intermediates across the OM. The type II system is broadly conserved in Gram-negative bacteria and involves a set of 12-16 different proteins named GspC-M, GspAB, GspN, GspO, and GspS. The type II secretion system is highly reminiscent of the type IV piliation assembly system. Based on findings about the subcellular localisation of the Gsp components, protein-protein interactions between Gsps and their multimerisation status, structural data and electron microscopy observation, it could be proposed a working model that strikingly runs both systems in parallel. (C) 2004 Elsevier B.V. All rights reserved.
引用
收藏
页码:163 / 179
页数:17
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