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Titolo:
Mapping the functional domains of HAP95, a protein that binds RNA helicaseA and activates the constitutive transport element of type D retroviruses
Autore:
Yang, JP; Tang, HL; Reddy, TR; Wong-Staal, F;
Indirizzi:
Univ Calif San Diego, Dept Biol, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 t Biol, La Jolla, CA 92093 USA Univ Calif San Diego, Dept Med, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 pt Med, La Jolla, CA 92093 USA
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 33, volume: 276, anno: 2001,
pagine: 30694 - 30700
SICI:
0021-9258(20010817)276:33<30694:MTFDOH>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-IMMUNODEFICIENCY-VIRUS; NUCLEAR EXPORT SIGNAL; POSTTRANSCRIPTIONAL REGULATION; HIV-1 REV; CRM1; TAP; IDENTIFICATION; PURIFICATION; REPLICATION; HOMOLOG;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
23
Recensione:
Indirizzi per estratti:
Indirizzo: Wong-Staal, F Univ Calif San Diego, Dept Biol, Stein Clin Res Bldg, La Jolla, CA 92093 USA Univ Calif San Diego Stein Clin Res Bldg La Jolla CA USA 92093
Citazione:
J.P. Yang et al., "Mapping the functional domains of HAP95, a protein that binds RNA helicaseA and activates the constitutive transport element of type D retroviruses", J BIOL CHEM, 276(33), 2001, pp. 30694-30700

Abstract

The complex retroviruses such as human immunodeficiency virus, type 1, employ a virally encoded protein, Rev, to mediate the nuclear export of unspliced and partially spliced mRNA. In contrast, the simian type D retrovirusesact through a cis-acting constitutive transport element (CTE) that presumably interacts directly with cellular export proteins. We first reported that RNA helicase A (RHA) is a shuttle protein that binds to functional CTE invitro and in vivo. Recently, we isolated a novel protein, HAP95, that specifically binds to the nuclear transport domain of RHA and up-regulates CTE-mediated gene expression. Here, using truncation and deletion mutations, wemapped the domains of HAP95 that are important for RHA binding, transactivation of CTE, and nuclear cytoplasmic shuttling. We report evidence for a novel nuclear export signal in HAP95 and showed that the domains involved inRHA binding and nuclear localization are required for CTE activation. Finally, we showed that HAP95 synergizes significantly with RHA on CTE-mediatedreporter gene expression and promotes nuclear export of unspliced mRNA in transfected cells. Taken together, these data support the proposal that HAP95 specifically facilitates CTE-mediated gene expression by directly binding to RHA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 01:59:41