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Titolo:
ACTIN POLYMERIZATION IS INDUCED BY ARP2 3 PROTEIN COMPLEX AT THE SURFACE OF LISTERIA-MONOCYTOGENES/
Autore:
WELCH MD; IWAMATSU A; MITCHISON TJ;
Indirizzi:
UNIV CALIF SAN FRANCISCO,DEPT CELLULAR & MOL PHARMACOL SAN FRANCISCO CA 94143 KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL YOKOHAMA KANAGAWA JAPAN
Titolo Testata:
Nature
fascicolo: 6613, volume: 385, anno: 1997,
pagine: 265 - 269
SICI:
0028-0836(1997)385:6613<265:APIIBA>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROLINE-RICH REGION; END-BOUND INSERTIN; MAMMALIAN-CELLS; BARBED ENDS; FILAMENTS; MOTILITY; PURIFICATION; ACANTHAMOEBA; MOVEMENT; PROFILIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
31
Recensione:
Indirizzi per estratti:
Citazione:
M.D. Welch et al., "ACTIN POLYMERIZATION IS INDUCED BY ARP2 3 PROTEIN COMPLEX AT THE SURFACE OF LISTERIA-MONOCYTOGENES/", Nature, 385(6613), 1997, pp. 265-269

Abstract

The pathogenic bacterium Listeria monocytogenes is capable of directed movement within the cytoplasm of infected host cells. Propulsion is thought to be driven by actin polymerization at the bacterial ceil surface(1,2), and moving bacteria leave in their wake a tail of actin filaments(3). Determining the mechanism by which L. monocytogenes polymerizes actin may aid the understanding of how actin polymerization is controlled in the cell. Actin assembly by L. monocytogenes requires the bacterial surface protein ActA(4,5) and protein components present in host cell cytoplasm. We have purified an eight-polypeptide complex that possesses the properties of the host-cell actin polymerization factor. The pure complex is sufficient to initiate ActA-dependent actin polymerization at the surface oft. monocytogenes, and is required to mediate actin tail formation and motility. Two subunits of this protein complex are actin-related proteins (ARPs) belonging to the Arp2 and Arp3subfamilies. The Arp3 subunit localizes to the surface of stationary bacteria and the tails of motile bacteria in tissue culture cells infected with L. monocytogenes; this is consistent with a role for the complex in promoting actin assembly in vivo. The activity and subunit composition of the Arp2/3 complex suggests that it forms a template that nucleates actin polymerization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 10:17:45