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Titolo:
UNEXPECTED STRUCTURAL REQUIREMENTS FOR GTPASE ACTIVITY OF THE INTERFERON-INDUCED MXA PROTEIN
Autore:
SCHWEMMLE M; RICHTER MF; HERRMANN C; NASSAR N; 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: 13518 - 13523
SICI:
0021-9258(1995)270:22<13518:USRFGA>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
ANTIVIRAL ACTIVITY; ESCHERICHIA-COLI; INFLUENZA-VIRUS; BINDING; LOCALIZATION; INHIBITION; MECHANISM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
28
Recensione:
Indirizzi per estratti:
Citazione:
M. Schwemmle et al., "UNEXPECTED STRUCTURAL REQUIREMENTS FOR GTPASE ACTIVITY OF THE INTERFERON-INDUCED MXA PROTEIN", The Journal of biological chemistry, 270(22), 1995, pp. 13518-13523

Abstract

MxA is an interferon-induced 76-kDa GTPase that inhibits the multiplication of several RNA viruses. Deleting seven amino acids from the COOH terminus reduced the GTPase activity of purified MxA to 1.4%. MxA mutants with COOH-terminal deletions of 63 or more amino acids lost all ability to hydrolyze GTP and failed to bind guanine nucleotides. By contrast, an MxA deletion mutant consisting of 301 amino acids from the NH2 terminus and 87 amino acids from the COOH terminus retained about 9% of wild-type GTPase activity, underscoring the pivotal role of COOH-terminal sequences. Limited proteolysis of wild-type MxA with proteinase K resulted in two resistant polypeptides of 60 and 10 kDa, respectively, which copurified as a stable complex. The p60-p10 complex exhibited high GTPase activity, suggesting that it included all MxA domainsrequired for this biochemical activity. Sequencing revealed that the NH2 terminus of the 60-kDa polypeptide mapped to leucine 41 and the NH2 terminus of the 10-kDa polypeptide to glutamine 564 of the MxA sequence. Based on these results we propose a model that suggests that the GTP-binding consensus element located in the NH2-terminal half of MxA is held in an active conformation by strong physical interactions withamino acids from the COOH-terminal region.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/01/20 alle ore 16:10:56