Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
MULTIMER FORMATION IS NOT ESSENTIAL FOR NUCLEAR EXPORT OF HUMAN T-CELL LEUKEMIA-VIRUS TYPE-1 REX TRANSACTIVATOR PROTEIN
Autore:
HEGER P; ROSORIUS O; KOCH C; CASARI G; GRASSMANN R; HAUBER J;
Indirizzi:
UNIV ERLANGEN NURNBERG,INST CLIN & MOL VIROL,SCHLOSSGARTEN 4 D-91054 ERLANGEN GERMANY UNIV ERLANGEN NURNBERG,INST CLIN & MOL VIROL D-91054 ERLANGEN GERMANY LION AG D-69120 HEIDELBERG GERMANY
Titolo Testata:
Journal of virology (Print)
fascicolo: 11, volume: 72, anno: 1998,
pagine: 8659 - 8668
SICI:
0022-538X(1998)72:11<8659:MFINEF>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
HTLV-I REX; RNA RESPONSE ELEMENTS; DOMINANT-NEGATIVE MUTANTS; HIV-1 REV; SEQUENCE REQUIREMENTS; REGULATORY PROTEINS; GENE-EXPRESSION; MESSENGER-RNA; LEUCINE ZIPPER; UNSPLICED RNA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
97
Recensione:
Indirizzi per estratti:
Citazione:
P. Heger et al., "MULTIMER FORMATION IS NOT ESSENTIAL FOR NUCLEAR EXPORT OF HUMAN T-CELL LEUKEMIA-VIRUS TYPE-1 REX TRANSACTIVATOR PROTEIN", Journal of virology (Print), 72(11), 1998, pp. 8659-8668

Abstract

The Rex trans-regulatory protein of human T-cell leukemia virus type 1 (HTLV-1) is required for the nuclear export of incompletely spliced and unspliced viral mRNAs and is therefore essential for virus replication. Rex is a nuclear phosphoprotein that directly binds to its cis acting Rex response element RNA target sequence and constantly shuttlesbetween the nucleus and cytoplasm. Moreover, Rex induces nuclear accumulation of unspliced viral RNA. Three protein domains which mediate nuclear import-RNA binding, nuclear export, and Rex oligomerization have been mapped within the 189-amino-acid Rex polypeptide. Here we identified a different region in the carboxy-terminal half of Rex which is also required for biological activity. In inactive mutants with mutations that map within this region, as well as in mutants that are deficient in Rex-specific multimerization, Rex trans activation could be reconstituted by fusion to a heterologous leucine zipper dimerization interface. The intracellular trafficking capabilities of wild-type and mutant Rex proteins reveal that biologically inactive and multimerization-deficient Rex mutants are still efficiently translocated from the nucleus to the cytoplasm. This observation indicates that multimerization is essential for Rex function but is not required for nuclear export. Finally, we are able to provide an improved model of the HTLV-1 Rex domain structure.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 14/08/20 alle ore 17:08:21