摘要
| 原文 | 英語 |
|---|---|
| 頁（從 - 到） | 6782-6793 |
| 頁數 | 12 |
| 期刊 | Journal of Virology |
| 卷 | 87 |
| 發行號 | 12 |
| DOIs | |
| 出版狀態 | 已發佈 - 六月 2013 |
| 對外發佈 | 是 |
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Kaposi's sarcoma-Associated herpesvirus (KSHV) latency-Associated nuclear antigen regulates the KSHV epigenome by association with the histone demethylase KDM3A. / Kim, K.Y.; Huerta, S.B.; Izumiya, C.; Wang, D.-H.; Martinez, A.; Shevchenko, B.; Kung, H.-J.; Campbell, M.; Izumiya, Y.
於: Journal of Virology, 卷 87, 編號 12, 06.2013, p. 6782-6793.研究成果: 雜誌貢獻 › 文章 › 同行評審
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TY - JOUR
T1 - Kaposi's sarcoma-Associated herpesvirus (KSHV) latency-Associated nuclear antigen regulates the KSHV epigenome by association with the histone demethylase KDM3A
AU - Kim, K.Y.
AU - Huerta, S.B.
AU - Izumiya, C.
AU - Wang, D.-H.
AU - Martinez, A.
AU - Shevchenko, B.
AU - Kung, H.-J.
AU - Campbell, M.
AU - Izumiya, Y.
N1 - 引用次數:30 Export Date: 5 March 2018 CODEN: JOVIA 通訊地址: Izumiya, Y.; Department of Dermatology, University of California, School of Medicine, Davis, United States; 電子郵件: yizumiya@ucdavis.edu 分析序列編號: GENBANK: NC_009333; 化學物質/CAS: Antigens, Viral; Histones; Jumonji Domain-Containing Histone Demethylases, 1.14.11.-; KDM3A protein, human, 1.14.11.-; Nuclear Proteins; latency-associated nuclear antigen 參考文獻: Cesarman, E., Chang, Y., Moore, P.S., Said, J.W., Knowles, D.M., Kaposi's sarcoma-associated herpesvirus-like DNA sequences in AIDS-related body-cavity-based lymphomas (1995) N. Engl. J. Med., 332, pp. 1186-1191; Dupin, N., Fisher, C., Kellam, P., Ariad, S., Tulliez, M., Franck, N., van Marck, E., Boshoff, C., Distribution of human herpesvirus-8 latently infected cells in Kaposi's sarcoma, multicentric Castleman's disease, and primary effusion lymphoma (1999) Proc. Natl. Acad. Sci. U.S.A., 96, pp. 4546-4551; Hu, J., Garber, A.C., Renne, R., The latency-associated nuclear antigen of Kaposi's sarcoma-associated herpesvirus supports latent DNA replication in dividing cells (2002) J. Virol., 76, pp. 11677-11687; Kelley-Clarke, B., De Leon-Vazquez, E., Slain, K., Barbera, A.J., Kaye, K.M., Role of Kaposi's sarcoma-associated herpesvirus C-terminal LANA chromosome binding in episome persistence (2009) J. Virol., 83, pp. 4326-4337; Kelley-Clarke, B., Ballestas, M.E., Komatsu, T., Kaye, K.M., Kaposi's sarcoma herpesvirus C-terminal LANA concentrates at pericentromeric and peri-telomeric regions of a subset of mitotic chromosomes (2007) Virology, 357, pp. 149-157; Komatsu, T., Ballestas, M.E., Barbera, A.J., Kelley-Clarke, B., Kaye, K.M., KSHV LANA1 binds DNA as an oligomer and residues N-terminal to the oligomerization domain are essential for DNA binding, replication, and episome persistence (2004) Virology, 319, pp. 225-236; Ye, F.C., Zhou, F.C., Yoo, S.M., Xie, J.P., Browning, P.J., Gao, S.J., Disruption of Kaposi's sarcoma-associated herpesvirus latent nuclear antigen leads to abortive episome persistence (2004) J. Virol., 78, pp. 11121-11129; Ganem, D., KSHV and the pathogenesis of Kaposi sarcoma: listening to human biology and medicine (2010) J. Clin. Invest., 120, pp. 939-949; Mesri, E.A., Cesarman, E., Boshoff, C., Kaposi's sarcoma and its associated herpesvirus (2010) Nat. Rev. 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PY - 2013/6
Y1 - 2013/6
N2 - Kaposi's sarcoma-associated herpesvirus (KSHV) latent genomes are tethered to host histones to form a minichromosome also known as an "episome." Histones, which are core components of chromatin, are heavily modified by various histone-targetingenzymes. Posttranslational modifications of histones significantly influence accessibility of transcriptional factors and thus have profound effects on gene expression. Recent studies showed that epigenetic marks on the KSHV episome are well organized, exemplified by the absence of histone H3 lysine 9 (H3K9) methylation, a heterochromatic histone mark, from immediate early andlatent gene promoters in naturally infected cells. The present study revealed a mechanistic insight into KSHV epigenome regulationvia a complex consisting of LANA and the H3K9me1/2 histone demethylase JMJD1A/KDM3A. This complex was isolatedfrom HeLa cell nuclear extracts stably expressing LANA and was verified by coimmunoprecipitation analyses and with purifiedproteins. LANA recruitment sites on the KSHV genome inversely correlated with H3K9me2 histone marks in naturally infectedcells, and methylation of H3K9 significantly inhibited LANA binding to the histone H3 tail. Chromatin immunoprecipitationcoupled with KSHV tiling arrays identified the recruitment sites of the complex, while depletion of LANA expression or overexpressionof a KDM3A binding-deficient mutant decreased KDM3A recruitment to the KSHV genome. Finally, ablation ofKDM3A expression from latently KSHV-infected cells significantly inhibited KSHV gene expression, leading to decreased KSHVreplication during reactivation. Taken together, our results suggest that LANA may play a role in regulation of epigenetic markson the KSHV genome, which is in part through association with the histone demethylase KDM3A. © 2013, American Society for Microbiology.
AB - Kaposi's sarcoma-associated herpesvirus (KSHV) latent genomes are tethered to host histones to form a minichromosome also known as an "episome." Histones, which are core components of chromatin, are heavily modified by various histone-targetingenzymes. Posttranslational modifications of histones significantly influence accessibility of transcriptional factors and thus have profound effects on gene expression. Recent studies showed that epigenetic marks on the KSHV episome are well organized, exemplified by the absence of histone H3 lysine 9 (H3K9) methylation, a heterochromatic histone mark, from immediate early andlatent gene promoters in naturally infected cells. The present study revealed a mechanistic insight into KSHV epigenome regulationvia a complex consisting of LANA and the H3K9me1/2 histone demethylase JMJD1A/KDM3A. This complex was isolatedfrom HeLa cell nuclear extracts stably expressing LANA and was verified by coimmunoprecipitation analyses and with purifiedproteins. LANA recruitment sites on the KSHV genome inversely correlated with H3K9me2 histone marks in naturally infectedcells, and methylation of H3K9 significantly inhibited LANA binding to the histone H3 tail. Chromatin immunoprecipitationcoupled with KSHV tiling arrays identified the recruitment sites of the complex, while depletion of LANA expression or overexpressionof a KDM3A binding-deficient mutant decreased KDM3A recruitment to the KSHV genome. Finally, ablation ofKDM3A expression from latently KSHV-infected cells significantly inhibited KSHV gene expression, leading to decreased KSHVreplication during reactivation. Taken together, our results suggest that LANA may play a role in regulation of epigenetic markson the KSHV genome, which is in part through association with the histone demethylase KDM3A. © 2013, American Society for Microbiology.
KW - histone demethylase
KW - histone H3
KW - latency associated nuclear antigen
KW - protein KDM3A
KW - unclassified drug
KW - amino terminal sequence
KW - article
KW - binding site
KW - chromatin immunoprecipitation
KW - complex formation
KW - controlled study
KW - embryo
KW - epigenetics
KW - gene control
KW - gene expression regulation
KW - genetic association
KW - histone methylation
KW - human
KW - human cell
KW - Human herpesvirus 8
KW - nonhuman
KW - nucleotide sequence
KW - priority journal
KW - protein binding
KW - protein expression
KW - protein protein interaction
KW - protein purification
KW - virus gene
KW - virus genome
KW - virus latency
KW - virus reactivation
KW - virus replication
KW - Antigens, Viral
KW - Chromatin Immunoprecipitation
KW - DNA Replication
KW - Epigenesis, Genetic
KW - Gene Expression Regulation, Viral
KW - Genome, Viral
KW - HEK293 Cells
KW - HeLa Cells
KW - Herpesvirus 8, Human
KW - Histones
KW - Host-Pathogen Interactions
KW - Humans
KW - Jumonji Domain-Containing Histone Demethylases
KW - Nuclear Proteins
KW - Oligonucleotide Array Sequence Analysis
KW - Virus Latency
U2 - 10.1128/JVI.00011-13
DO - 10.1128/JVI.00011-13
M3 - Article
VL - 87
SP - 6782
EP - 6793
JO - Journal of Virology
JF - Journal of Virology
SN - 0022-538X
IS - 12
ER -