@prefix prodottidellaricerca: . @prefix istituto: . @prefix prodotto: . istituto:CDS040 prodottidellaricerca:prodotto prodotto:ID27573 . @prefix pubblicazioni: . @prefix unitaDiPersonaleInterno: . unitaDiPersonaleInterno:MATRICOLA8735 pubblicazioni:autoreCNRDi prodotto:ID27573 . @prefix modulo: . modulo:ID2691 prodottidellaricerca:prodotto prodotto:ID27573 . @prefix rdf: . prodotto:ID27573 rdf:type prodotto:TIPO1101 . @prefix retescientifica: . prodotto:ID27573 rdf:type retescientifica:ProdottoDellaRicerca . @prefix rdfs: . prodotto:ID27573 rdfs:label "Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase. (Articolo in rivista)"@en . @prefix xsd: . prodotto:ID27573 pubblicazioni:anno "2009-01-01T00:00:00+01:00"^^xsd:gYear . @prefix skos: . prodotto:ID27573 skos:altLabel "
Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G. (2009)
Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase.
in Nucleic acids research
"^^rdf:HTML ; pubblicazioni:autori "Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G."^^xsd:string ; pubblicazioni:paginaInizio "36660"^^xsd:string ; pubblicazioni:paginaFine "36669"^^xsd:string ; pubblicazioni:numeroVolume "37"^^xsd:string . @prefix ns11: . prodotto:ID27573 pubblicazioni:rivista ns11:ID337255 ; skos:note "ISI Web of Science (WOS)"^^xsd:string ; pubblicazioni:titolo "Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase."^^xsd:string ; prodottidellaricerca:abstract "The HIV-1 accessory protein Vif plays a dual role: it counteracts the natural restriction factors APOBEC3G and 3F and ensures efficient retrotranscription of the HIV-1 RNA genome. We have previously shown that Vif can act as an auxiliary factor for HIV-1 reverse transcriptase (RT), increasing its rate of association to RNA or DNA templates. Here, by using seven different Vif mutants, we provide in vitro evidences that Vif stimulates HIV-1 RT through direct protein-protein interaction, which is mediated by its C-terminal domain. Physical interaction appears to require the proline-rich region comprised between amino acid (aa) 161 and 164 of Vif, whereas the RT stimulatory activity requires, in addition, the extreme C-terminal region (aa 169-192) of the Vif protein. Neither the RNA interaction domain, nor the Zn(++)-binding domain of Vif are required for its interaction with the viral RT. Pseudotyped HIV-1 lentiviral vectors bearing Vif mutants deleted in the RNA- or RT-binding domains show defects in retrotranscription/integration processes in both permissive and nonpermissive cells. Our results broaden our knowledge on how three important functions of Vif (RNA binding, RT binding and stimulation and Zn(++) binding), are coordinated by different domains." ; prodottidellaricerca:prodottoDi istituto:CDS040 , modulo:ID2691 ; pubblicazioni:autoreCNR unitaDiPersonaleInterno:MATRICOLA8735 . ns11:ID337255 pubblicazioni:rivistaDi prodotto:ID27573 .