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
相关论文
共 151 条
  • [21] MOLECULAR ANALYSIS OF THE MAJOR CELLULASE (CELV) OF ERWINIA-CAROTOVORA - EVIDENCE FOR AN EVOLUTIONARY MIX-AND-MATCH OF ENZYME DOMAINS
    COOPER, VJC
    SALMOND, GPC
    [J]. MOLECULAR AND GENERAL GENETICS, 1993, 241 (3-4): : 341 - 350
  • [22] plcR1 and plcR2 are putative calcium binding proteins required for secretion of the hemolytic phospholipase C of Pseudomonas aeruginosa
    CotaGomez, A
    Vasil, AI
    Kadurugamuwa, J
    Beveridge, TJ
    Schweizer, HP
    Vasil, ML
    [J]. INFECTION AND IMMUNITY, 1997, 65 (07) : 2904 - 2913
  • [23] The Salmonella typhimurium InvH protein is an outer membrane lipoprotein required for the proper localization of InvG
    Daefler, S
    Russel, M
    [J]. MOLECULAR MICROBIOLOGY, 1998, 28 (06) : 1367 - 1380
  • [24] The C-terminal domain of the secretin PulD contains the binding site for its cognate chaperone, PulS, and confers PulS dependence on plV(f1) function
    Daefler, S
    Guilvout, I
    Hardie, KR
    Pugsley, AP
    Russel, M
    [J]. MOLECULAR MICROBIOLOGY, 1997, 24 (03) : 465 - 475
  • [25] Convergence of the secretory pathways for cholera toxin and the filamentous phage, CTXφ
    Davis, BM
    Lawson, EH
    Sandkvist, M
    Ali, A
    Sozhamannan, S
    Waldor, MK
    [J]. SCIENCE, 2000, 288 (5464) : 333 - 335
  • [26] Molecular organization of the xcp gene cluster in Pseudomonas putida:: absence of an xcpX (gspK) homologue
    de Groot, A
    Gerritse, G
    Tommassen, J
    Lazdunski, A
    Filloux, A
    [J]. GENE, 1999, 226 (01) : 35 - 40
  • [27] Exchange of Xcp (Gsp) secretion machineries between Pseudomonas aeruginosa and Pseudomonas alcaligenes:: Species specificity unrelated to substrate recognition
    De Groot, A
    Koster, M
    Gérard-Vincent, M
    Gerritse, G
    Lazdunski, A
    Tommassen, J
    Filloux, A
    [J]. JOURNAL OF BACTERIOLOGY, 2001, 183 (03) : 959 - 967
  • [28] The bacterial translocase: a dynamic protein channel complex
    de Keyzer, J
    van der Does, C
    Driessen, AJM
    [J]. CELLULAR AND MOLECULAR LIFE SCIENCES, 2003, 60 (10) : 2034 - 2052
  • [29] Identification of a novel Gsp-related pathway required for secretion of the manganese-oxidizing factor of Pseudomonas putida strain GB-1
    de Vrind, J
    de Groot, A
    Brouwers, GJ
    Tommassen, J
    de Vrind-de Jong, E
    [J]. MOLECULAR MICROBIOLOGY, 2003, 47 (04) : 993 - 1006
  • [30] Characterization of type II protein secretion (xcp) genes in the plant growth stimulating Pseudomonas putida, strain WCS358
    deGroot, A
    Krijger, JJ
    Filloux, A
    Tommassen, J
    [J]. MOLECULAR AND GENERAL GENETICS, 1996, 250 (04): : 491 - 504