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Titolo:
EFFECTS OF TRANSLATION INITIATION-FACTOR EIF-5A ON THE FUNCTIONING OFHUMAN T-CELL LEUKEMIA-VIRUS TYPE-I REX AND HUMAN-IMMUNODEFICIENCY-VIRUS REV INHIBITED TRANS DOMINANTLY BY A REX MUTANT DEFICIENT IN RNA-BINDING
Autore:
KATAHIRA J; ISHIZAKI T; SAKAI H; ADACHI A; SHIDA H;
Indirizzi:
KYOTO UNIV,INST VIRUS RES KYOTO 606 JAPAN KYOTO UNIV,INST VIRUS RES KYOTO 606 JAPAN ST MARIANNA UNIV,SCH MED,INST MED SCI KAWASAKI KANAGAWA 216 JAPAN
Titolo Testata:
Journal of virology
fascicolo: 5, volume: 69, anno: 1995,
pagine: 3125 - 3133
SICI:
0022-538X(1995)69:5<3125:EOTIEO>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
EUKARYOTIC PROTEIN-SYNTHESIS; LONG TERMINAL REPEAT; GENE-EXPRESSION REQUIRES; VIRAL MESSENGER-RNA; HIV-1 REV; HTLV-I; RESPONSE ELEMENT; ACTIVATION DOMAIN; TARGET SEQUENCE; NUCLEOLAR LOCALIZATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
76
Recensione:
Indirizzi per estratti:
Citazione:
J. Katahira et al., "EFFECTS OF TRANSLATION INITIATION-FACTOR EIF-5A ON THE FUNCTIONING OFHUMAN T-CELL LEUKEMIA-VIRUS TYPE-I REX AND HUMAN-IMMUNODEFICIENCY-VIRUS REV INHIBITED TRANS DOMINANTLY BY A REX MUTANT DEFICIENT IN RNA-BINDING", Journal of virology, 69(5), 1995, pp. 3125-3133

Abstract

The viral transactivator proteins Rex and Rev are necessary for the expression of structural proteins of human T-cell leukemia virus type Iand human immunodeficiency virus type 1, respectively. Although the interaction of Rex/Rev with a cellular cofactor(s) has been thought to be required for Rex/Rev action, there is no suitable system to search for the cofactor(s) in mammalian cells. We found that a Rex mutant, TAgRex, which contains a simian virus 40 nuclear localization signal in place of the N-terminal 19 amino acids of Rex, could dominantly inhibit wild-type Rex/Rev functions. The inhibition did not require either Rev response element/Rex response element binding or the oligomerization ability of the mutant, but it did require a region around amino acid90 of the Rex protein, suggesting that TAgRex sequestered the cellular cofactor. Complementation with the eukaryotic translation initiationfactor 5A (eIF-5A) in this system could restore the impaired Rex function. These results indicate that eIF-5A is the cofactor indispensablefor Rex function. Additionally, by using a two-hybrid system, the homo-oligomer formation of Rex was found to be mediated by the region around amino acid 90 in addition to Tyr-64 and Trp-65 of Rex protein. Thus, eIF-SA may play a part in the formation of the Rex homo oligomer.

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Documento generato il 21/09/20 alle ore 06:21:44