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Titolo:
Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri
Autore:
Page, AL; Fromont-Racine, M; Sansonetti, P; Legrain, P; Parsot, C;
Indirizzi:
Inst Pasteur, INSERM, U389, Unite Pathogenie Microbienne Mol, F-75724 Paris 15, France Inst Pasteur Paris France 15 e Microbienne Mol, F-75724 Paris 15, France Inst Pasteur, Unite Genet Interact Macromol, F-75724 Paris, France Inst Pasteur Paris France F-75724 teract Macromol, F-75724 Paris, France
Titolo Testata:
MOLECULAR MICROBIOLOGY
fascicolo: 4, volume: 42, anno: 2001,
pagine: 1133 - 1145
SICI:
0950-382X(200111)42:4<1133:COTIPO>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
B-CELL EPITOPES; EPITHELIAL-CELLS; YERSINIA-ENTEROCOLITICA; MAMMALIAN-CELLS; INTERACTION MAP; IPAC INVASINS; ENTRY; PLASMID; YOPE; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
46
Recensione:
Indirizzi per estratti:
Indirizzo: Parsot, C Inst Pasteur, INSERM, U389, Unite Pathogenie Microbienne Mol, 25-28 Rue Docteur Roux, F-75724 Paris 15, France Inst Pasteur 25-28 Rue Docteur Roux Paris France 15 15, France
Citazione:
A.L. Page et al., "Characterization of the interaction partners of secreted proteins and chaperones of Shigella flexneri", MOL MICROB, 42(4), 2001, pp. 1133-1145

Abstract

The type III secretion (TTS) system of Gram-negative pathogenic bacteria is composed of proteins that assemble into the TTS machinery, proteins that are secreted by this machinery and specific chaperones that are required for storage and sometimes secretion of these proteins. Many sequential protein interactions are involved in the TTS pathway to deliver effector proteinsto host cells. We used the yeast two-hybrid system to investigate the interaction partners of the Shigella flexneri effectors and chaperones. Libraries of preys containing random fusions with fragments of the TTS proteins were screened using effectors and chaperones as baits. Interactions between the effectors IpaB and lpaC and their chaperone IpgC were detected by this method, and interaction domains were identified. Using a His-tagged IpgC protein to co-purify truncated IpaB and lpaC proteins, we showed that the chaperone-binding domain was unique and located in the N-terminus of these proteins. This domain was not required for the secretion of recombinant proteins but was involved in the stability of lpaC and instability of IpaB. Homotypic interactions were identified with the baits IpaA, IpaB and IpaC. Interactions between effectors and components of the TTS machinery were also selected that might give insights into regulation of the TTS process.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 22:42:31