MOMP (major outer membrane protein) of Campylobacter jejuni;: a versatile pore-forming protein

被引:42
作者
Dé, E
Jullien, M
Labesse, G
Pagès, JM
Molle, G
Bolla, JM
机构
[1] Fac Med Marseille, INSERM, CJF 96 06, F-13385 Marseille 05, France
[2] Univ Mediterranee, F-13385 Marseille, France
[3] Univ Rouen, Fac Sci, IFRMP 23, CNRS,UMR 6522, F-76821 Mt St Aignan, France
[4] Fac Pharm Montpellier, INSERM, U414, CNRS,UMR 9955, F-34060 Montpellier, France
关键词
porin quaternary structure; channel-forming property; structure/function relationship;
D O I
10.1016/S0014-5793(00)01244-8
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 great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into monomers without disrupting their folded conformation. The porin of Campylobacter jejuni, however, displays two folded structures, a classical oligomer and a monomer resistant to detergent denaturation. We probed the transition of trimer to monomer using light scattering experiments and examined the secondary structures of these two molecular states by infra-red spectroscopy. The channel-forming properties of both trimer and monomer were studied after incorporation into artificial lipid bilayers, In these conditions, the trimer induced ion channels with a conductance value of 1200 pS in 1 M NaCl. The pores showed marked cationic selectivity and sensitivity to low voltage. Analysis of the isolated monomer showed nearly the same single-channel conductance and the same selectivity and sensitivity to voltage. These results indicate that the folded monomer form of C. jejuni MOMP displays essentially the same pore-forming properties as the native trimer. (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:93 / 97
页数:5
相关论文
共 33 条
[1]   Electron microscopy of the major outer membrane protein of Campylobacter jejuni [J].
Amako, K ;
Wai, SN ;
Umeda, A ;
Shigematsu, M ;
Takade, A .
MICROBIOLOGY AND IMMUNOLOGY, 1996, 40 (10) :749-754
[2]   SEROLOGICAL DIVERSITY AND CHEMICAL STRUCTURES OF CAMPYLOBACTER-JEJUNI LOW-MOLECULAR-WEIGHT LIPOPOLYSACCHARIDES [J].
ASPINALL, GO ;
MCDONALD, AG ;
RAJU, TS ;
PANG, H ;
MILLS, SD ;
KURJANCZYK, L ;
PENNER, JL .
JOURNAL OF BACTERIOLOGY, 1992, 174 (04) :1324-1332
[3]   Voltage-gating of Escherichia coli porin:: A cystine-scanning mutagenesis study of loop 3 [J].
Bainbridge, G ;
Mobasheri, H ;
Armstrong, GA ;
Lea, EJA ;
Lakey, JH .
JOURNAL OF MOLECULAR BIOLOGY, 1998, 275 (02) :171-176
[4]   THE ASSEMBLY OF THE MAJOR OUTER-MEMBRANE PROTEIN OMPF OF ESCHERICHIA-COLI DEPENDS ON LIPID-SYNTHESIS [J].
BOLLA, JM ;
LAZDUNSKI, C ;
PAGES, JM .
EMBO JOURNAL, 1988, 7 (11) :3595-3599
[5]   CONFORMATIONAL-ANALYSIS OF THE CAMPYLOBACTER-JEJUNI PORIN [J].
BOLLA, JM ;
LORET, E ;
ZALEWSKI, M ;
PAGES, JM .
JOURNAL OF BACTERIOLOGY, 1995, 177 (15) :4266-4271
[6]   Dynamic light scattering study of precrystallizing ribonuclease solutions [J].
Boyer, M ;
Roy, MO ;
Jullien, M .
JOURNAL OF CRYSTAL GROWTH, 1996, 167 (1-2) :212-220
[7]   ASYMMETRY OF ORIENTATION AND VOLTAGE GATING OF THE ACIDOVORAX-DELAFIELDII PORIN OMP34 IN LIPID BILAYERS [J].
BRUNEN, M ;
ENGELHARDT, H .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1993, 212 (01) :129-135
[8]  
BUEHLER LK, 1991, J BIOL CHEM, V266, P24446
[9]   CRYSTAL-STRUCTURES EXPLAIN FUNCTIONAL-PROPERTIES OF 2 ESCHERICHIA-COLI PORINS [J].
COWAN, SW ;
SCHIRMER, T ;
RUMMEL, G ;
STEIERT, M ;
GHOSH, R ;
PAUPTIT, RA ;
JANSONIUS, JN ;
ROSENBUSCH, JP .
NATURE, 1992, 358 (6389) :727-733
[10]   Lipopolysaccharides and divalent cations are involved in the formation of an assembly-competent intermediate of outer-membrane protein PhoE of E-coli [J].
deCock, H ;
Tommassen, J .
EMBO JOURNAL, 1996, 15 (20) :5567-5573