New insight into the molecular mechanisms of two-partner secretion

被引:53
作者
Mazar, Joseph [1 ]
Cotter, Peggy A. [1 ]
机构
[1] Univ Calif Santa Barbara, Dept Mol Cellular & Dev Biol, Santa Barbara, CA 93106 USA
关键词
D O I
10.1016/j.tim.2007.10.005
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
Two-partner secretion (TPS) systems, which export large proteins to the surface and/or extracellular milieu of Gram-negative bacteria, are members of a large superfamily of protein translocation systems that are widely distributed in animals, plants and fungi, in addition to nearly all groups of Gram-negative bacteria. Recent intense research on TPS systems has provided new insight into the structure and topology of the outer membrane translocator proteins and the large exoproteins that they secrete, the interactions between them, and mechanisms for retention of some of the secreted proteins on the bacterial surface. Evidence for secretion-dependant folding of mature exoproteins has also been obtained. Together, these findings provide a deeper understanding of the molecular mechanisms underlying these simple but elegant secretion systems.
引用
收藏
页码:508 / 515
页数:8
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共 53 条
[21]   Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin [J].
Jacob-Dubuisson, F ;
El-Hamel, C ;
Saint, N ;
Guédin, S ;
Willery, E ;
Molle, G ;
Locht, C .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (53) :37731-37735
[22]   Protein secretion through autotransporter and two-partner pathways [J].
Jacob-Dubuisson, F ;
Fernandez, R ;
Coutte, L .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2004, 1694 (1-3) :235-257
[23]   Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins [J].
Jacob-Dubuisson, F ;
Locht, C ;
Antoine, R .
MOLECULAR MICROBIOLOGY, 2001, 40 (02) :306-313
[24]   Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin [J].
JacobDubuisson, F ;
Buisine, C ;
Mielcarek, N ;
Clement, E ;
Menozzi, FD ;
Locht, C .
MOLECULAR MICROBIOLOGY, 1996, 19 (01) :65-78
[25]   Lack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineries [J].
JacobDubuisson, F ;
Buisine, C ;
Willery, E ;
RenauldMongenie, G ;
Locht, C .
JOURNAL OF BACTERIOLOGY, 1997, 179 (03) :775-783
[26]   The turn of the screw:: Variations of the abundant β-solenoid motif in passenger domains of Type V secretory proteins [J].
Kajava, Andrey V. ;
Steven, Alasdair C. .
JOURNAL OF STRUCTURAL BIOLOGY, 2006, 155 (02) :306-315
[27]   Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins [J].
Kajava, AV ;
Cheng, N ;
Cleaver, R ;
Kessel, M ;
Simon, MN ;
Willery, E ;
Jacob-Dubuisson, F ;
Locht, C ;
Steven, AC .
MOLECULAR MICROBIOLOGY, 2001, 42 (02) :279-292
[28]   The haemolysin-secreting ShIB protein of the outer membrane of Serratia marcescens:: determination of surface-exposed residues and formation of ion-permeable pores by ShIB mutants in artificial lipid bilayer membranes [J].
Könninger, UW ;
Hobbie, S ;
Benz, R ;
Braun, V .
MOLECULAR MICROBIOLOGY, 1999, 32 (06) :1212-1225
[29]   An essential role of Sam50 in the protein sorting and assembly machinery of the mitochondrial outer membrane [J].
Kozjak, V ;
Wiedemann, N ;
Milenkovic, D ;
Lohaus, C ;
Meyer, HE ;
Guiard, B ;
Meisinger, C ;
Pfanner, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (49) :48520-48523
[30]   N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin [J].
Lambert-Buisine, C ;
Willery, E ;
Locht, C ;
Jacob-Dubuisson, F .
MOLECULAR MICROBIOLOGY, 1998, 28 (06) :1283-1293