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Article: The DNA architectural protein HMGB1 facilitates RTA-mediated viral gene expression in gamma-2 herpesviruses

TitleThe DNA architectural protein HMGB1 facilitates RTA-mediated viral gene expression in gamma-2 herpesviruses
Authors
Issue Date2004
Citation
Journal of Virology, 2004, v. 78, n. 23, p. 12940-12950 How to Cite?
AbstractReplication and transcription activator (RTA), an immediate-early gene product of gamma-2 herpesviruses including Kaposi's sarcoma-associated herpesvirus (KSHV) and murine gamma herpesvirus 68 (MHV-68), plays a critical role in controlling the viral life cycle. RTA acts as a strong transcription activator for several downstream genes of KSHV and MHV-68 through direct DNA binding, as well as via indirect mechanisms. HMGB1 (also called HMG-1) protein is a highly conserved nonhistone chromatin protein with the ability to bind and bend DNA. HMGB1 protein promoted RTA binding to different RTA target sites in vitro, with greater enhancement to low-affinity sites than to high-affinity sites. Box A or box B and homologues of HMGB1 also enhanced RTA binding to DNA. Transient transfection of HMGB1 stimulated RTA transactivation of RTA-responsive promoters from KSHV and MHV-68. Furthermore, MHV-68 viral gene expression, as well as viral replication, was significantly reduced in HMGB1-deficient cells than in the wild type. This abated viral gene expression was partially restored by HMGB1 transfection into HMGB1-/- cells. These results suggest an important function of the DNA architectural protein, HMGB1, in RTA-mediated gene expression, as well as viral replication in gamma-2 herpesviruses.
Persistent Identifierhttp://hdl.handle.net/10722/285876
ISSN
2023 Impact Factor: 4.0
2023 SCImago Journal Rankings: 1.378
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorMoon, Jung Song-
dc.contributor.authorHwang, Seungmin-
dc.contributor.authorWong, Wendy-
dc.contributor.authorRound, June-
dc.contributor.authorMartinez-Guzman, Dee Ann-
dc.contributor.authorTurpaz, Yaron-
dc.contributor.authorLiang, Jie-
dc.contributor.authorWong, Ben-
dc.contributor.authorJohnson, Reid C.-
dc.contributor.authorCarey, Michael-
dc.contributor.authorSun, Ren-
dc.date.accessioned2020-08-18T04:56:53Z-
dc.date.available2020-08-18T04:56:53Z-
dc.date.issued2004-
dc.identifier.citationJournal of Virology, 2004, v. 78, n. 23, p. 12940-12950-
dc.identifier.issn0022-538X-
dc.identifier.urihttp://hdl.handle.net/10722/285876-
dc.description.abstractReplication and transcription activator (RTA), an immediate-early gene product of gamma-2 herpesviruses including Kaposi's sarcoma-associated herpesvirus (KSHV) and murine gamma herpesvirus 68 (MHV-68), plays a critical role in controlling the viral life cycle. RTA acts as a strong transcription activator for several downstream genes of KSHV and MHV-68 through direct DNA binding, as well as via indirect mechanisms. HMGB1 (also called HMG-1) protein is a highly conserved nonhistone chromatin protein with the ability to bind and bend DNA. HMGB1 protein promoted RTA binding to different RTA target sites in vitro, with greater enhancement to low-affinity sites than to high-affinity sites. Box A or box B and homologues of HMGB1 also enhanced RTA binding to DNA. Transient transfection of HMGB1 stimulated RTA transactivation of RTA-responsive promoters from KSHV and MHV-68. Furthermore, MHV-68 viral gene expression, as well as viral replication, was significantly reduced in HMGB1-deficient cells than in the wild type. This abated viral gene expression was partially restored by HMGB1 transfection into HMGB1-/- cells. These results suggest an important function of the DNA architectural protein, HMGB1, in RTA-mediated gene expression, as well as viral replication in gamma-2 herpesviruses.-
dc.languageeng-
dc.relation.ispartofJournal of Virology-
dc.titleThe DNA architectural protein HMGB1 facilitates RTA-mediated viral gene expression in gamma-2 herpesviruses-
dc.typeArticle-
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1128/JVI.78.23.12940-12950.2004-
dc.identifier.pmid15542646-
dc.identifier.pmcidPMC524970-
dc.identifier.scopuseid_2-s2.0-8644232572-
dc.identifier.volume78-
dc.identifier.issue23-
dc.identifier.spage12940-
dc.identifier.epage12950-
dc.identifier.isiWOS:000225087500022-
dc.identifier.issnl0022-538X-

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