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Titolo:
INTERFERON-INDUCED MXA PROTEIN - GTP-BINDING AND GTP HYDROLYSIS PROPERTIES
Autore:
RICHTER MF; SCHWEMMLE M; HERRMANN C; WITTINGHOFER A; STAEHELI P;
Indirizzi:
UNIV FREIBURG,INST MED MIKROBIOL & HYG,DEPT VIROL,VIROL ABT,HERMANN HERDER STR 11 D-79008 FREIBURG GERMANY UNIV FREIBURG,INST MED MIKROBIOL & HYG,DEPT VIROL,VIROL ABT D-79008 FREIBURG GERMANY MAX PLANCK INST MOLEK PHYSIOL,STRUKT BIOL ABT D-44139 DORTMUND GERMANY
Titolo Testata:
The Journal of biological chemistry
fascicolo: 22, volume: 270, anno: 1995,
pagine: 13512 - 13517
SICI:
0021-9258(1995)270:22<13512:IMP-GA>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
DYNAMIN GTPASE; NUCLEOTIDE-FREE; DOMAINS; P21; MICROTUBULES; EXPRESSION; KINETICS; SHIBIRE; VIRUS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
M.F. Richter et al., "INTERFERON-INDUCED MXA PROTEIN - GTP-BINDING AND GTP HYDROLYSIS PROPERTIES", The Journal of biological chemistry, 270(22), 1995, pp. 13512-13517

Abstract

MxA is a GTPase encoded by an interferon-activated human gene which inhibits the multiplication of several RNA viruses. Recombinant histidine-tagged MxA protein (His-MxA) was expressed in Escherichia coli and purified to near homogeneity. Gel filtration showed that it formed high molecular weight oligomers. Purified His-MxA exhibited specific GTP hydrolysis rates of up to 350 nmol of GTP/min/mg of protein, corresponding to a turnover number of 27 min(-1). The K-m for this reaction was260 mu M. Guanine nucleotides did not copurify with His-MxA. Binding experiments in solution with fluorescent-labeled nucleotides confirmedthat His-MxA binds guanine nucleotides rather weakly and further showed that the fluorescent GDP analog N-methylanthraniloyl (mant)-GDP hada much lower affinity for His-MxA (K-d 20 mu M, k(off) 8.5 s(-1)) than the nonhydrolyzable GTP analog mant-5'-guanylyl-beta,gamma-imidotriphosphate (mant-GMP-PNP) (K-d 0.75 mu M, k(off) 0.012 s(-1)). Competitive binding studies with nonlabeled nucleotides revealed a similar binding preference of His-MxA for GTP over GDP: the K-d for GTP was 20 mu M, whereas the K-d for GDP was 100 mu M. Thus, a high percentage of MxA molecules may be complexed with GTP in vivo.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 10:00:00