2004 Fiscal Year Final Research Report Summary
Core histone modifications change the higher order of DNA structurec resulting in its biological output
| Project/Area Number |
15390098
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
General medical chemistry
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| Research Institution | Nagasaki University |
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Principal Investigator |
ITO Takashi Nagasaki University, Graduate School of Biomedical Sciences, Professor, 大学院・医歯薬学総合研究科, 教授 (90306275)
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| Co-Investigator(Kenkyū-buntansha) |
IKEHARA Tsuyoshi Nagasaki University, Graduate School of Biomedical Sciences, Assistant Professor, 大学院・医歯薬学総合研究科, 講師 (90359951)
NAKAGAWA Takeya Nagasaki University, Graduate School of Biomedical Sciences, Research Associate, 大学院・医歯薬学総合研究科, 助手 (50363502)
YASUI Kiyoshi Nagasaki University, Graduate School of Biomedical Sciences, Research Associate, 大学院・医歯薬学総合研究科, 助手 (50372777)
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| Project Period (FY) |
2003 – 2004
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| Keywords | histone / acetylation / phosphorylation / nucleosome / chromatin / transcription |
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| Research Abstract |
In the eukaryotic nucleus, DNA exists as a nucleoprotein complex termed chromatin. The work is based on the hypothesis that chromatin dynamics and structure are an integral component of the analysis of DNA-dependent processes. Posttranslational histone modifications are important for the regulation of many biological phenomena. In this project, we clafified that a precise role for histone acetylation, namely to alter the structure of nucleosomes and facilitate the loss of H2A-H2B dimmers that have been previously remodeled by the action of ATP-dependent chromatin remodeling complexes. We also clarified that transcription from chromatin templates is ordered and sequential, with precise timing and roles for ATP-dependent chromatin remodeling, subsequent histone acetylation and alterations in nucleosome structure. In addition we found that histone H2A is phosphorylated by unique kinase. We found that NHK-1-catalyzed phosphorylation of a conserved serine/threonine residue in H2A is a new component of the histone code which might be related to cell cycle progression.
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[Journal Article] Nucleosomal histone kinase-1 phosphorylates H2A Thr 119 during mitosis in the early Drosophila embryo.2004
Author(s)
Aihara, H., Nakagawa, T., Yasui, K., Ohta, T., Hirose, S., Dhomae, N., Takio, K., Kaneko, M., Takeshima, Y., Muramatsu, M., Ito, T.
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Journal Title
Genes Dev 18
Pages: 877-888
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] A Pitfall in Diagnosis of Human Prion Diseases Using Detection of Protease-resistant Prion Protein in Urine : CONTAMINATION WITH BACTERIAL OUTER MEMBRANE PROTEINS.2004
Author(s)
Furukawa, H., Doh-Ura, K., Okuwaki, R., Shirabe, S., Yamamoto, K., Udono, H., Ito, T., Katamine, S., Niwa, M.
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Journal Title
J Biol Chem 279
Pages: 23661-23667
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Isoflavones stimulate estrogen receptor-mediated core histone acetylation.2004
Author(s)
Hong, T., Nakagawa, T., Pan, W., Kim, M.Y., Kraus, W.L, Ikehara, T., Yasui, K., Aihara, H., Takebe, M., Muramatsu, M., Ito, T.
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Journal Title
Biochem Biophys Res Commun 317
Pages: 259-264
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] Identification of ser-386 of interferon regulatory factor 3 as critical target for inducible phosphorylation that determines activation.2004
Author(s)
Mori, M., Yoneyama, M., Ito, T., Takahashi, K., Inagaki, F., Fujita, T.
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Journal Title
J Biol Chem 279
Pages: 9698-9702
Description
「研究成果報告書概要(欧文)」より
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[Journal Article] The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome.2003
Author(s)
Kitagawa, H., Fujiki, R., Yoshimura, K., Mezaki, Y., Uematsu, Y., Matsui, D., Ogawa, S., Unno, K., Okubo, M., Tokita, A., Nakagawa, T., Ito, T.et al.
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Description
「研究成果報告書概要(和文)」より
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[Journal Article] The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome.2003
Author(s)
Kitagawa, H., Fujiki, R., Yoshimura, K., Mezaki, Y., Uematsu, Y., Matsui, D., Ogawa, S., Unno, K., Okubo, M., Tokita, A., Nakagawa, T., Ito, T., Ishimi, Y., Nagasawa, H., Matsumoto, T., Yanagisawa, J., Kato, S.
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