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Titolo:
THE ACTIVATION DOMAIN OF SIMIAN IMMUNODEFICIENCY VIRUS SIVMAC239 REV PROTEIN IS STRUCTURALLY AND FUNCTIONALLY ANALOGOUS TO THE HIV-1 REV ACTIVATION DOMAIN
Autore:
BERCHTOLD S; HORNUNG U; AEPINUS C;
Indirizzi:
UNIV ERLANGEN NURNBERG,INST KLIN & MOLEK VIROL,SCHLOSSGARTEN 4 D-91054 ERLANGEN GERMANY UNIV ERLANGEN NURNBERG,INST KLIN & MOLEK VIROL D-91054 ERLANGEN GERMANY
Titolo Testata:
Virology
fascicolo: 1, volume: 211, anno: 1995,
pagine: 290 - 295
SICI:
0042-6822(1995)211:1<290:TADOSI>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
VIRAL MESSENGER-RNA; GENE-EXPRESSION REQUIRES; TRANS-ACTIVATOR; RESPONSIVE ELEMENT; TARGET SEQUENCE; TYPE-1 AFFECTS; BINDING; REGION; IDENTIFICATION; LEUKEMIA;
Tipo documento:
Note
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
60
Recensione:
Indirizzi per estratti:
Citazione:
S. Berchtold et al., "THE ACTIVATION DOMAIN OF SIMIAN IMMUNODEFICIENCY VIRUS SIVMAC239 REV PROTEIN IS STRUCTURALLY AND FUNCTIONALLY ANALOGOUS TO THE HIV-1 REV ACTIVATION DOMAIN", Virology, 211(1), 1995, pp. 290-295

Abstract

The Rev proteins of primate immunodeficiency viruses are essential transactivators for the switch from early to late phase in the viral replication cycle. By mutational analysis, a putative activation domain (AD) has been assigned to the carboxy-terminus. This leucine-rich stretch of amino acids proved to be essential for the transactivating properties of HIV-1 Rev. Some mutants in the AD transdominantly inhibit thefunction of wild-type Rev protein very efficiently. We identified a similar domain structure for SIVmac239 Rev by sequence comparison and in vitro mutagenesis. The leucine/isoleucine residues of the SIVmac239 Rev activation domain appeared to be of similar importance for function. The mutants of these residues in the SIV AD displayed a dominant negative phenotype on both HIV-1 and SIVmac 239 rev-responsive elements (RRE). The prokaryotically expressed wild-type and mutant proteins were analyzed for RNA-binding properties in a gel-shift assay in vitro. This assay revealed a similar binding pattern of wild-type and transdominant proteins on either RRE. (C) 1995 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/09/20 alle ore 07:57:56