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Titolo:
IDENTIFICATION OF THE ACTIVATION DOMAIN OF EQUINE INFECTIOUS-ANEMIA VIRUS REV
Autore:
FRIDELL RA; PARTIN KM; CARPENTER S; CULLEN BR;
Indirizzi:
DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710 DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT MICROBIOL DURHAM NC 27710 DUKE UNIV,MED CTR,GENET SECT DURHAM NC 27710 IOWA STATE UNIV SCI & TECHNOL,COLL VET MED,DEPT MICROBIOL IMMUNOL & PREVENT MED AMES IA 50011
Titolo Testata:
Journal of virology
fascicolo: 12, volume: 67, anno: 1993,
pagine: 7317 - 7323
SICI:
0022-538X(1993)67:12<7317:IOTADO>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
STRUCTURAL GENE-EXPRESSION; FELINE IMMUNODEFICIENCY VIRUS; VIRAL MESSENGER-RNA; TYPE-1 REV; TRANS-ACTIVATOR; HIV-1 REV; FUNCTIONAL-ANALYSIS; I REX; NUCLEOTIDE-SEQUENCE; TARGET SEQUENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
44
Recensione:
Indirizzi per estratti:
Citazione:
R.A. Fridell et al., "IDENTIFICATION OF THE ACTIVATION DOMAIN OF EQUINE INFECTIOUS-ANEMIA VIRUS REV", Journal of virology, 67(12), 1993, pp. 7317-7323

Abstract

Several members of the lentivirus family of complex retroviruses havebeen shown to encode proteins that are functionally equivalent to theRev posttranscriptional regulatory protein of human immunodeficiency virus type 1 (HIV-1). Furthermore, the domain organization of HIV-1 Rev, featuring a highly basic N-terminal RNA binding domain and a leucine-rich C-terminal effector domain, has also been shown to be highly conserved among Rev proteins derived from not only the primate but also the ovine and caprine lentiviruses. Although it has therefore appearedhighly probable that the lentivirus equine infectious anemia virus (EIAV) also encodes a Rev, the predicted amino acid sequence of this putative EIAV regulatory protein does not display any evident homology tothe basic and leucine-rich motifs characteristic of other known Rev proteins. By fusion of different segments of the proposed EIAV Rev protein to the well-defined RNA binding domain of either HIV-1 or visna virus Rev, we have identified a segment of this EIAV protein that can efficiently substitute in cis for the otherwise essential activation motif. Interestingly, the minimal EIAV Rev activation motif identified inthis study comprises approximately 18 amino acids located toward the protein N terminus that lack any evident similarity to the leucine-rich activation domains found in these other lentivirus Rev proteins. It therefore appears that the Rev protein of EIAV, while analogous in function to Rev proteins defined in lentiviruses of primate, ovine, and caprine origin, is nevertheless distinguished by an entirely novel domain organization.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 17:42:28