Phosphorylation of purified recombinant hepatitis B virus-X protein by mitogen-activated protein kinase and protein kinase C in vitro

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dc.contributor.authorYoung Ik Lee-
dc.contributor.authorSun Ok Kim-
dc.contributor.authorHyok Joon Kwon-
dc.contributor.authorJong Gu Park-
dc.contributor.authorMi Jin Sohn-
dc.contributor.authorSoon Seok Jeong-
dc.date.accessioned2017-04-19T08:58:16Z-
dc.date.available2017-04-19T08:58:16Z-
dc.date.issued2001-
dc.identifier.issn0166-0934-
dc.identifier.uri10.1016/S0166-0934(00)00282-2ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5535-
dc.description.abstractThe recombinant human hepatitis B virus-X protein (rhHBx) has been expressed as inclusion bodies in Escherichia coli and purified. By sequential dialysis of urea, rhHBx was folded into the native structure, which was demonstrated by both the efficacy of its transcriptional activation of the adenovirus major late promoter, fluorescence and circular dichroism (CD) analysis. The increase in CD values at 220 nm and a corresponding blue shift of the intrinsic fluorescence emission confirmed the ability of HBx to refold in lower concentrations of urea to produce the active protein. After purification and renaturation, the rhHBx protein was found to be phosphorylated by protein kinase C (PKC) and mitogen-activated protein kinase (MAPK). In vivo phosphorylation of HBx was also demonstrated. Although PKC and MAPK enhance the HBx phosphorylation in vitro, neither protein kinase A nor caseine kinase II (CKII) phosphorylate HBx protein, though there are possible substrate residues of both kinases in HBx protein. Phosphoamino acid analysis of the total acid hydrolyzed HBx showed that serine residues can be phosphorylated by PKC or MAPK.-
dc.publisherElsevier-
dc.titlePhosphorylation of purified recombinant hepatitis B virus-X protein by mitogen-activated protein kinase and protein kinase C in vitro-
dc.title.alternativePhosphorylation of purified recombinant hepatitis B virus-X protein by mitogen-activated protein kinase and protein kinase C in vitro-
dc.typeArticle-
dc.citation.titleJournal of Virological Methods-
dc.citation.number1-
dc.citation.endPage10-
dc.citation.startPage1-
dc.citation.volume95-
dc.contributor.affiliatedAuthorYoung Ik Lee-
dc.contributor.affiliatedAuthorSun Ok Kim-
dc.contributor.affiliatedAuthorHyok Joon Kwon-
dc.contributor.affiliatedAuthorMi Jin Sohn-
dc.contributor.affiliatedAuthorSoon Seok Jeong-
dc.contributor.alternativeName이영익-
dc.contributor.alternativeName김선옥-
dc.contributor.alternativeName권혁준-
dc.contributor.alternativeName박종구-
dc.contributor.alternativeName손미진-
dc.contributor.alternativeName정순석-
dc.identifier.bibliographicCitationJournal of Virological Methods, vol. 95, no. 1, pp. 1-10-
dc.identifier.doi10.1016/S0166-0934(00)00282-2-
dc.subject.keywordhepatitis B virus-X protein-
dc.subject.keywordcircular dichroism-
dc.subject.keywordprotein kinase C-
dc.subject.keywordmitogen-activated protein kinase-
dc.subject.localhepatitis B virus X protein-
dc.subject.localHepatitis B virus-X protein-
dc.subject.localHepatitis B virus X protein-
dc.subject.localhepatitis B virus-X protein-
dc.subject.localHepatitis B virus X-protein-
dc.subject.localcircular dichroism-
dc.subject.localCircular dichroism-
dc.subject.localProtein kinase C-
dc.subject.localprotein kinase C-
dc.subject.localprotein kinase c-
dc.subject.localmitogen-activated protein kinase-
dc.subject.localMitogen activated protein kinase-
dc.subject.localMitogen-activated protein (MAP) kinase-
dc.subject.localmitogen-activated protein kinases-
dc.subject.localMitogen-activated protein kinase (MAPK)-
dc.subject.localMitogen-activated protein kinase-
dc.subject.localMitogenactivated protein kinase-
dc.subject.localmitogen activated protein kinase-
dc.subject.localMitogen-activated protein kinases (MAPKs)-
dc.subject.localMitogen-acti-vated protein kinase-
dc.subject.localMitogen-activated protein kinases-
dc.description.journalClassY-
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