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Titolo:
Activation of the superoxide-generating NADPH oxidase by chimeric proteinsconsisting of segments of the cytosolic component p67(phox) and the small GTPase Rac1
Autore:
Alloul, N; Gorzalczany, Y; Itan, M; Sigal, N; Pick, E;
Indirizzi:
Tel Aviv Univ, Sackler Sch Med, Julius Friedrich Cohnheim Minerva Ctr Phagocyte R, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978cyte R, IL-69978 Tel Aviv, Israel Tel Aviv Univ, Sackler Sch Med, Ela Kodesz Inst Host Def Infect Dis, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 ct Dis, IL-69978 Tel Aviv, Israel
Titolo Testata:
BIOCHEMISTRY
fascicolo: 48, volume: 40, anno: 2001,
pagine: 14557 - 14566
SICI:
0006-2960(200112)40:48<14557:AOTSNO>2.0.ZU;2-S
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-FREE SYSTEM; RESPIRATORY BURST OXIDASE; SODIUM DODECYL-SULFATE; EFFECTOR REGION; INSERT REGION; IN-VITRO; DOMAIN; BINDING; IDENTIFICATION; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Pick, E Tel Aviv Univ, Sackler Sch Med, Julius Friedrich Cohnheim Minerva Ctr Phagocyte R, IL-69978 Tel Aviv, Israel Tel Aviv Univ Tel Aviv Israel IL-69978 IL-69978 Tel Aviv, Israel
Citazione:
N. Alloul et al., "Activation of the superoxide-generating NADPH oxidase by chimeric proteinsconsisting of segments of the cytosolic component p67(phox) and the small GTPase Rac1", BIOCHEM, 40(48), 2001, pp. 14557-14566

Abstract

Activation of the superoxide (O-2(-))-generating NADPH oxidase of phagocytes is the consequence of the assembly of a membrane-associated flavocytochrome b(559) with the cytosolic proteins p47(phox) and p67(phox) and the small GTPase Rac (1 or 2). We proposed that Rac I serves as a membrane-targeting molecule for p67(phox). This hypothesis was tested by constructing recombinant chimeric proteins, joining various functional domains of p67(phox) and Rac 1, and expressing these in Escherichia coli. Chimeras were assayed for the ability to support O-2(-) production by phagocyte membranes in an amphiphile-activated cell-free system in the presence or absence of p47phox. Achimera consisting of p67(phox) truncated at residue 212 and fused to a full-length Rac1 [p67(phox)(1-212)-Rac1(1-192)] was a potent NADPH oxidase activator. A p67(phox)(1-212)-Rac1(178-192) chimera, to which Rac1 contributed only the C-terminal polybasic domain, was a weaker but consistent activator. Chimeras comprising the full length of Rae I bound GTP/ GDP, like bona fide GTPases, The activity of p67(phox)-Rac1 chimeras was dependent on the presence of the tetratricopeptide repeat and activation domains, in the p67(phox) segment, and on an intact polybasic region, at the C terminus of theRac1 segment, but not on the insert region of Rac1. Partial activation by chimeras, in the GTP-bound form, was also possible in the absence of p47(phox). Evidence is offered in support of the proposal that the GTP- and GDP-bound forms of chimera p67phox(1 -212)-Rac1 (1 - 192) have distinct conformations, corresponding to the presence and absence of intrachimeric bonds, respectively.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/07/20 alle ore 22:36:36