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Titolo:
MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein
Autore:
De, E; Jullien, M; Labesse, G; Pages, JM; Molle, G; Bolla, JM;
Indirizzi:
Fac Med Marseille, INSERM, CJF 96 06, F-13385 Marseille 05, France Fac MedMarseille Marseille France 05 6 06, F-13385 Marseille 05, France Univ Mediterranee, F-13385 Marseille, France Univ Mediterranee MarseilleFrance F-13385 ee, F-13385 Marseille, France Univ Rouen, Fac Sci, IFRMP 23, CNRS,UMR 6522, F-76821 Mt St Aignan, FranceUniv Rouen Mt St Aignan France F-76821 522, F-76821 Mt St Aignan, France Fac Pharm Montpellier, INSERM, U414, CNRS,UMR 9955, F-34060 Montpellier, France Fac Pharm Montpellier Montpellier France F-34060 060 Montpellier, France
Titolo Testata:
FEBS LETTERS
fascicolo: 1, volume: 469, anno: 2000,
pagine: 93 - 97
SICI:
0014-5793(20000303)469:1<93:M(OMPO>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
ESCHERICHIA-COLI PORIN; OMPF; PHOE; LIPOPOLYSACCHARIDES; IDENTIFICATION; INTERMEDIATE; DEPENDENCE; MUTANTS; TRIMER; SIZE;
Keywords:
porin quaternary structure; channel-forming property; structure/function relationship;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Bolla, JM Fac Med Marseille, INSERM, CJF 96 06, 27 Bd Jean Moulin, F-13385Marseille05, France Fac Med Marseille 27 Bd Jean Moulin Marseille France 05 France
Citazione:
E. De et al., "MOMP (major outer membrane protein) of Campylobacter jejuni; a versatile pore-forming protein", FEBS LETTER, 469(1), 2000, pp. 93-97

Abstract

The great majority of trimeric porins of Gram-negative bacteria cannot be dissociated into monomers without disrupting their folded conformation. Theporin 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 experimentsand 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 19:09:34