YaeT-independent multimerization and outer membrane association of secretin PulD

被引:46
作者
Collin, Severine
Guilvout, Ingrid
Chami, Mohamed
Pugsley, Anthony P.
机构
[1] Inst Pasteur, URA2172, Mol Genet Unit, F-75724 Paris 15, France
[2] Inst Pasteur, URA2172, CNRS, F-75724 Paris 15, France
[3] Univ Basel, Muller Inst, Biozentrum, CH-4056 Basel, Switzerland
关键词
D O I
10.1111/j.1365-2958.2007.05743.x
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
Previous studies demonstrated that targeting of the dodecameric secretin PulD to the Escherichia coli outer membrane is strictly dependent on the chaperone-like pilotin PulS. Here, we report that PulD multimerization and membrane association in strains producing PulS were unaffected when the levels of the essential outer membrane assembly factor YaeT(Omp85) were reduced by controlled expression of a paraBAD-yaeT transcriptional fusion. This behaviour contrasted markedly to that of the trimeric porin LamB, which remained monomeric under these conditions. Furthermore, resistance to extraction by the detergent Sarkosyl and by urea, and susceptibility to trypsin digestion all suggested that PulD localized to the outer membrane in YaeT-depleted cells. We conclude that, unlike classical beta-barrel outer membrane proteins such as LamB, multimerization of PulD is largely YaeT-independent.
引用
收藏
页码:1350 / 1357
页数:8
相关论文
共 33 条
[1]   Secretins take shape [J].
Bayan, N ;
Guilvout, I ;
Pugsley, AP .
MOLECULAR MICROBIOLOGY, 2006, 60 (01) :1-4
[2]   MAJOR HEAT-MODIFIABLE OUTER-MEMBRANE PROTEIN IN GRAM-NEGATIVE BACTERIA - COMPARISON WITH THE OMPA PROTEIN OF ESCHERICHIA-COLI [J].
BEHER, MG ;
SCHNAITMAN, CA ;
PUGSLEY, AP .
JOURNAL OF BACTERIOLOGY, 1980, 143 (02) :906-913
[3]   Secretins of Pseudomonas aeruginosa:: large holes in the outer membrane [J].
Bitter, W .
ARCHIVES OF MICROBIOLOGY, 2003, 179 (05) :307-314
[4]   Formation of oligomeric rings by XcpQ and PilQ, which are involved in protein transport across the outer membrane of Pseudomonas aeruginosa [J].
Bitter, W ;
Koster, M ;
Latijnhouwers, M ;
de Cock, H ;
Tommassen, J .
MOLECULAR MICROBIOLOGY, 1998, 27 (01) :209-219
[5]   Type IV pilus biogenesis in Neisseria meningitidis:: PilW is involved in a step occurring after pilus assembly, essential for fibre stability and function [J].
Carbonnelle, E ;
Hélaine, S ;
Prouvensier, L ;
Nassif, X ;
Pelicic, V .
MOLECULAR MICROBIOLOGY, 2005, 55 (01) :54-64
[6]   Structural insights into the secretin PulD and its trypsin-resistant core [J].
Chami, M ;
Guilvout, I ;
Gregorini, M ;
Rémigy, HW ;
Müller, SA ;
Valerio, M ;
Engel, A ;
Pugsley, AP ;
Bayan, N .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (45) :37732-37741
[7]   Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 Å resolution [J].
Collins, RF ;
Frye, SA ;
Kitmitto, A ;
Ford, RC ;
Tonjum, T ;
Derrick, JP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (38) :39750-39756
[8]  
DENFERT C, 1989, J BIOL CHEM, V264, P17462
[9]   CLONING AND EXPRESSION IN ESCHERICHIA-COLI OF THE KLEBSIELLA-PNEUMONIAE GENES FOR PRODUCTION, SURFACE LOCALIZATION AND SECRETION OF THE LIPOPROTEIN PULLULANASE [J].
DENFERT, C ;
RYTER, A ;
PUGSLEY, AP .
EMBO JOURNAL, 1987, 6 (11) :3531-3538
[10]   Loss of outer membrane proteins without inhibition of lipid export in an Escherichia coli YaeT mutant [J].
Doerrler, WT ;
Raetz, CRH .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (30) :27679-27687