Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
INTERACTIONS BETWEEN SINDBIS VIRUS RNAS AND A 68 AMINO-ACID DERIVATIVE OF THE VIRAL CAPSID PROTEIN FURTHER DEFINES THE CAPSID BINDING-SITE
Autore:
WEISS B; GEIGENMULLERGNIRKE U; SCHLESINGER S;
Indirizzi:
WASHINGTON UNIV,SCH MED,DEPT MOLEC MICROBIOL,660 S EUCLID AVE ST LOUIS MO 63110 WASHINGTON UNIV,SCH MED,DEPT MOLEC MICROBIOL,660 S EUCLID AVE ST LOUIS MO 63110
Titolo Testata:
Nucleic acids research
fascicolo: 5, volume: 22, anno: 1994,
pagine: 780 - 786
SICI:
0305-1048(1994)22:5<780:IBSVRA>2.0.ZU;2-T
Fonte:
ISI
Lingua:
ENG
Soggetto:
GENE-EXPRESSION REQUIRES; PACKAGING SIGNAL; COAT PROTEIN; LEUKEMIA-VIRUS; ENCAPSIDATION; SEQUENCE; TYPE-1; SPECIFICITY; MUTAGENESIS; MUTATIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
37
Recensione:
Indirizzi per estratti:
Citazione:
B. Weiss et al., "INTERACTIONS BETWEEN SINDBIS VIRUS RNAS AND A 68 AMINO-ACID DERIVATIVE OF THE VIRAL CAPSID PROTEIN FURTHER DEFINES THE CAPSID BINDING-SITE", Nucleic acids research, 22(5), 1994, pp. 780-786

Abstract

In previous studies of encapsidation of Sindbis virus RNA, we identified a 570nt fragment (nt 684 - 1253) from the 12 kb genome that binds to the viral capsid protein with specificity and is required for packaging of Sindbis virus defective interfering RNAs. We now show that thecapsid binding activity resides in a highly structured 132nt fragment(nt 945-1076). We had also demonstrated that a 68 amino acid peptide derived from the capsid protein retained most of the binding activity of the original protein and have now developed an RNA mobility shift assay with this peptide fused to glutathione-S-transferase. We have used this assay in conjunction with the original assay in which the intact capsid protein was immobilized on nitrocellulose to analyze more extensive deletions in the 132-mer. All of the deletions led to a reduction in binding, but the binding of a 5' 67-mer was enhanced by the addition of nonspecific flanking sequences. This result suggests that the stability of a particular structure within the 132nt sequence may be important for capsid recognition.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 07:55:13