Recent progress and future directions in studies of the main terminal branch of the general secretory pathway in Gram-negative bacteria - A review

被引:85
作者
Pugsley, AP
Francetic, O
Possot, OM
Sauvonnet, N
Hardie, KR
机构
关键词
protein secretion; outer membrane; Type-IV pilins; multimeric protein complexes; chaperone; secretion signal; pullulanase;
D O I
10.1016/S0378-1119(96)00803-7
中图分类号
Q3 [遗传学];
学科分类号
071007 ; 090102 ;
摘要
The main terminal branch (MTB) of the general secretory pathway is used by a wide variety of Gram(-) bacteria to transport exoproteins from the periplasm to the outside milieu. Recent work has led to the identification of the function of two of its 14 (or more) components: an enzyme with type-IV prepilin peptidase activity and a chaperone-like protein required for the insertion of another of the MTB components into the outer membrane. Despite these important discoveries, little tangible progress has been made towards identifying MTB components that determine secretion specificity (presumably by binding to cognate exoproteins) or which form the putative channel through which exoproteins are transported across the outer membrane. However, the idea that the single integral outer membrane component of the MTB could line the wall of this channel, and the intriguing possibility that other components of the MTB form a rudimentary type-IV pilus-like structure that might span the periplasm both deserve more careful examination. Although Escherichia coli K-12 does not normally secrete exoproteins, its chromosome contains an apparently complete set of genes coding for MTB components. At least two of these genes code for functional proteins, but the operon in which twelve of the genes are located does not appear to be expressed. We are currently searching for conditions which allow these genes to be expressed with the eventual aim of identifying the protein(s) that E. coli K-12 can secrete. (C) 1997 Elsevier Science B.V.
引用
收藏
页码:13 / 19
页数:7
相关论文
共 60 条
[1]   XCP-MEDIATED PROTEIN SECRETION IN PSEUDOMONAS-AERUGINOSA - IDENTIFICATION OF 2 ADDITIONAL GENES AND EVIDENCE FOR REGULATION OF XCP GENE-EXPRESSION [J].
AKRIM, M ;
BALLY, M ;
BALL, G ;
TOMMASSEN, J ;
TEERINK, H ;
FILLOUX, A ;
LAZDUNSKI, A .
MOLECULAR MICROBIOLOGY, 1993, 10 (02) :431-443
[2]   CLONING, SEQUENCING, AND MAPPING OF THE BACTERIOFERRITIN GENE (BFR) OF ESCHERICHIA-COLI K-12 [J].
ANDREWS, SC ;
HARRISON, PM ;
GUEST, JR .
JOURNAL OF BACTERIOLOGY, 1989, 171 (07) :3940-3947
[3]   PROTEIN SECRETION IN PSEUDOMONAS-AERUGINOSA - CHARACTERIZATION OF 7 XCP GENES AND PROCESSING OF SECRETORY APPARATUS COMPONENTS BY PREPILIN PEPTIDASE [J].
BALLY, M ;
FILLOUX, A ;
AKRIM, M ;
BALL, G ;
LAZDUNSKI, A ;
TOMMASSEN, J .
MOLECULAR MICROBIOLOGY, 1992, 6 (09) :1121-1131
[4]   PROTEIN SECRETION IN PSEUDOMONAS-AERUGINOSA - THE XCPA GENE ENCODES AN INTEGRAL INNER MEMBRANE-PROTEIN HOMOLOGOUS TO KLEBSIELLA-PNEUMONIAE SECRETION FUNCTION PROTEIN PULO [J].
BALLY, M ;
BALL, G ;
BADERE, A ;
LAZDUNSKI, A .
JOURNAL OF BACTERIOLOGY, 1991, 173 (02) :479-486
[5]  
BORTOLIGERMAN I, 1995, J MOL BIOL, V246, P82, DOI 10.1006/jmbi.1994.0068
[6]   PERIPLASMIC DISULFIDE BOND FORMATION IS ESSENTIAL FOR CELLULASE SECRETION BY THE PLANT PATHOGEN ERWINIA-CHRYSANTHEMI [J].
BORTOLIGERMAN, I ;
BRUN, E ;
PY, B ;
CHIPPAUX, M ;
BARRAS, F .
MOLECULAR MICROBIOLOGY, 1994, 11 (03) :545-553
[7]   Role of the propeptide in folding and secretion of elastase of Pseudomonas aeruginosa [J].
Braun, P ;
Tommassen, J ;
Filloux, A .
MOLECULAR MICROBIOLOGY, 1996, 19 (02) :297-306
[8]   SOME OF THE OUT GENES INVOLVED IN THE SECRETION OF PECTATE LYASES IN ERWINIA-CHRYSANTHEMI ARE REGULATED BY KDGR [J].
CONDEMINE, G ;
DOREL, C ;
HUGOUVIEUXCOTTEPATTAT, N ;
ROBERTBAUDOUY, J .
MOLECULAR MICROBIOLOGY, 1992, 6 (21) :3199-3211
[9]  
DECOCK H, 1990, J BIOL CHEM, V265, P4646
[10]  
DENFERT C, 1989, J BIOL CHEM, V264, P17462