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Titolo:
THE INFLUENZA-VIRUS NS1 PROTEIN FORMS MULTIMERS IN-VITRO AND IN-VIVO
Autore:
NEMEROFF ME; QIAN XY; KRUG RM;
Indirizzi:
RUTGERS STATE UNIV,DEPT MOLEC BIOL & BIOCHEM PISCATAWAY NJ 08855 RUTGERS STATE UNIV,DEPT MOLEC BIOL & BIOCHEM PISCATAWAY NJ 08855
Titolo Testata:
Virology
fascicolo: 2, volume: 212, anno: 1995,
pagine: 422 - 428
SICI:
0042-6822(1995)212:2<422:TINPFM>2.0.ZU;2-L
Fonte:
ISI
Lingua:
ENG
Soggetto:
REV TRANS-ACTIVATOR; GENE-EXPRESSION REQUIRES; VIRAL MESSENGER-RNA; HIV-1 REV; TARGET SEQUENCE; BINDING-SITE; REGION; OLIGOMERIZATION; INVITRO;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
27
Recensione:
Indirizzi per estratti:
Citazione:
M.E. Nemeroff et al., "THE INFLUENZA-VIRUS NS1 PROTEIN FORMS MULTIMERS IN-VITRO AND IN-VIVO", Virology, 212(2), 1995, pp. 422-428

Abstract

The NS1 protein of the influenza A virus inhibits both the nuclear export of mRNA and pre-mRNA splicing. Two functional domains, an RNA-binding domain and an effector domain, have been identified in this protein. Here we demonstrate that the NS1 protein exists as a dimer in vitro both in the absence of its RNA target and when it is bound to a specific RNA target, U6 snRNA. This indicates that it is most likely the dimer that binds to the RNA target. Mutational analysis indicated that the RNA-binding and dimerization domains are coincident. Multimerization also occurs in vivo, as assayed using the yeast two-hybrid system. In contrast to the situation in vitro, multimerization in vivo was mediated by not only the RNA-binding domain but also the effector domain. This suggests that multimerization in vivo involves a cellular protein cofactor that bridges more than one NS1 protein molecule together via their effector domains. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 06:47:15