Brasil | Artículos de revistas
dc.creatorRui E.
dc.creatorDe Moura P.R.
dc.creatorKobarg J.
dc.date2001
dc.date2015-06-26T14:43:04Z
dc.date2015-11-26T14:15:51Z
dc.date2015-06-26T14:43:04Z
dc.date2015-11-26T14:15:51Z
dc.date.accessioned2018-03-28T21:16:48Z
dc.date.available2018-03-28T21:16:48Z
dc.identifier
dc.identifierVirus Research. , v. 74, n. 1-2, p. 59 - 73, 2001.
dc.identifier1681702
dc.identifier10.1016/S0168-1702(00)00245-8
dc.identifierhttp://www.scopus.com/inward/record.url?eid=2-s2.0-0035114391&partnerID=40&md5=488573b9e9680a08528be3e23dc3a0da
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/94967
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/94967
dc.identifier2-s2.0-0035114391
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1242906
dc.descriptionThe hepatitis B virus protein HBx has been implicated in the development of liver cancer. It has been shown that the HBx protein is able to bind to single-stranded DNA in a specific manner. This DNA binding activity might be relevant for HBx oncogene character. To study the HBx interaction with nucleic acids in more detail we expressed full-length HBx as well as several N- and C-terminally truncated HBx proteins as 6xHis and GST-fusions in E. coli. Using a gel shift assay, we were able to demonstrate that all of the truncated HBx proteins have the ability to bind to an AU-rich RNA. The affinity of GST-HBx #3 (residues 80-142) was an order of magnitude higher than that of GST-HBx #2 (residues 5-79), indicating that a high affinity RNA binding site is located in HBx C-terminal half. AUF1 is the protein ligand that binds to AU-rich RNA regions present in certain proto-oncogene mRNAs and causes their rapid degradation. By a competitive binding experiment of AUF1 and HBx to the AU-rich RNA oligonucleotide, we show that HBx is able to displace AUF1 from its binding site on the RNA oligonucleotide. This new aspect of HBx function is discussed in the context of cellular transformation. © 2001 Elsevier Science B.V.
dc.description74
dc.description1-2
dc.description59
dc.description73
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dc.languageen
dc.publisher
dc.relationVirus Research
dc.rightsfechado
dc.sourceScopus
dc.titleExpression Of Deletion Mutants Of The Hepatitis B Virus Protein Hbx In E. Coli And Characterization Of Their Rna Binding Activities
dc.typeArtículos de revistas


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