The cysteine residues of the hepatitis B virus onco-protein HBx are not required for its interaction with RNA or with human p53

dc.creatorde Moura, PR
dc.creatorRui, E
dc.creatorGoncalves, KD
dc.creatorKobarg, J
dc.date2005
dc.dateMAR
dc.date2014-11-14T01:59:48Z
dc.date2015-11-26T16:03:51Z
dc.date2014-11-14T01:59:48Z
dc.date2015-11-26T16:03:51Z
dc.date.accessioned2018-03-28T22:53:04Z
dc.date.available2018-03-28T22:53:04Z
dc.identifierVirus Research. Elsevier Science Bv, v. 108, n. 41671, n. 121, n. 131, 2005.
dc.identifier0168-1702
dc.identifierWOS:000227083700014
dc.identifier10.1016/j.virusres.2004.08.018
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/74897
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/74897
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/74897
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1265362
dc.descriptionThe hepatitis B virus (HBV) protein HBx has been implicated to induce liver cancer in transgenic mice and transactivates a variety of viral and cellular promoters. The 17 kDa protein HBx consists of 154 amino acids, contains 10 cysteine residues and is translated during the viral infection. It has been shown previously that the HBx protein is able to bind to singlestranded DNA and RNA. This nucleic acid binding activity might be relevant for HBx oncogenic character. Furthermore, HBx has been reported to interact with a series of cellular proteins, especially with transcription factors, including the tumor suppressor protein p53. To evaluate the importance of the cysteine residues in HBx for its interaction with RNA and p53 we expressed full-length HBx-wt as well as several truncated mini-HBx(18-142) proteins with multiple cysteine to serine point mutations as 6xHis fusion proteins in Escherichia coli. Using UV cross-linking assays we demonstrate that all truncated mini-HBx proteins with cysteine/serine point mutations maintained the ability to bind to an AU-38 RNA oligonucleotide. Furthermore, we performed in vitro binding assays of selected HBx mutants with GST-p53, circular dichroism spectroscopic analysis of the mutant HBx protein secondary structure and a p53 based transcription activation assay in yeast cells. In summary, our data suggest that the cysteine residues in the HBx protein are of minor importance for its interaction with both RNA and the p53 protein. (C) 2004 Elsevier B.V. All rights reserved.
dc.description108
dc.description41671
dc.description121
dc.description131
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationVirus Research
dc.relationVirus Res.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectviral hepatitis
dc.subjecthepatocellular carcinoma
dc.subjectviral transactivator
dc.subjectoncogene
dc.subjectTumor-suppressor Gene
dc.subjectX-protein
dc.subjectBinding-protein
dc.subjectDna-binding
dc.subjectTranscriptional Activation
dc.subjectEscherichia-coli
dc.subjectTransgenic Mice
dc.subjectAlpha-subunit
dc.subjectExpression
dc.subjectTransactivation
dc.titleThe cysteine residues of the hepatitis B virus onco-protein HBx are not required for its interaction with RNA or with human p53
dc.typeArtículos de revistas


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