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Titolo:
PROTEIN-SEQUENCE REQUIREMENTS FOR FUNCTION OF THE HUMAN T-CELL LEUKEMIA-VIRUS TYPE-1 REX NUCLEAR EXPORT SIGNAL DELINEATED BY A NOVEL IN-VIVO RANDOMIZATION-SELECTION ASSAY
Autore:
BOGERD HP; FRIDELL RA; BENSON RE; HUA J; CULLEN BR;
Indirizzi:
DUKE UNIV,MED CTR,HOWARD HUGHES MED INST,BOX 3025,ROOM 426 CARL BLDG,RES DR DURHAM NC 27710 DUKE UNIV,MED CTR,HOWARD HUGHES MED INST DURHAM NC 27710 DUKE UNIV,MED CTR,DEPT GENET DURHAM NC 27710
Titolo Testata:
Molecular and cellular biology
fascicolo: 8, volume: 16, anno: 1996,
pagine: 4207 - 4214
SICI:
0270-7306(1996)16:8<4207:PRFFOT>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
HTLV-I REX; GENE-EXPRESSION REQUIRES; INFECTIOUS-ANEMIA VIRUS; RNA RESPONSE ELEMENTS; VIRAL MESSENGER-RNA; STEM-LOOP STRUCTURE; IMMUNODEFICIENCY-VIRUS; REGULATORY PROTEINS; ACTIVATION DOMAIN; TRANS-ACTIVATOR;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
41
Recensione:
Indirizzi per estratti:
Citazione:
H.P. Bogerd et al., "PROTEIN-SEQUENCE REQUIREMENTS FOR FUNCTION OF THE HUMAN T-CELL LEUKEMIA-VIRUS TYPE-1 REX NUCLEAR EXPORT SIGNAL DELINEATED BY A NOVEL IN-VIVO RANDOMIZATION-SELECTION ASSAY", Molecular and cellular biology, 16(8), 1996, pp. 4207-4214

Abstract

The Rex protein of human T-cell leukemia virus type 1, like the functionally equivalent Rev protein of human immunodeficiency virus type 1,contains a leucine-rich activation domain that specifically interactswith the human nucleoporin-like Rab/hRIP cofactor. Here, this Rex sequence is shown to function also as a protein nuclear export signal (NES). Rex sequence libraries containing randomized forms of the activation domain/ NES were screened for retention of the ability to bind Rab/hRIP by using the yeast two-hybrid assay. While the selected sequencesdiffered widely in primary sequence, all were functional as Rex activation domains. In contrast, randomized sequences that failed to bind Rab/hRIP lacked Rex activity. The selected sequences included one with homology to the Rev activation domain/NES and a second that was similar to the NES found in the cellular protein kinase inhibitor or. A highly variant, yet fully active, activation domain sequence selected on the basis of Rab/hRIP binding retained full NES function even though this sequence preserved only a single leucine residue. In contrast, nonfunctional activation domain mutants that were unable to bind Rab/hRIP had also lost NES function. These data demonstrate that NES activity is a defining characteristic of the activation domains found in the Rev/Rex class of retroviral regulatory proteins and strongly support the hypothesis that the Rab/hRIP cofactor plays a critical role in mediating the biological activity of these NESs. In addition, these data suggest a consensus sequence for NESs of the Rev/Rex class.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 26/09/20 alle ore 08:25:47