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Mcl1, DNA polymerase α accessory factor, is required for two distinct domain structures in fission yeast centromere
https://ir.soken.ac.jp/records/1021
https://ir.soken.ac.jp/records/1021aa8e91dd-82e8-4d1f-9c45-f502fe51de04
| 名前 / ファイル | ライセンス | アクション |
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要旨・審査要旨 (334.3 kB)
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本文 (18.9 MB)
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| Item type | 学位論文 / Thesis or Dissertation(1) | |||||
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| 公開日 | 2010-02-22 | |||||
| タイトル | ||||||
| タイトル | Mcl1, DNA polymerase α accessory factor, is required for two distinct domain structures in fission yeast centromere | |||||
| タイトル | ||||||
| タイトル | Mcl2, DNA polymerase α accessory factor, is required for two distinct domain structures in fission yeast centromere | |||||
| 言語 | en | |||||
| 言語 | ||||||
| 言語 | eng | |||||
| 資源タイプ | ||||||
| 資源タイプ識別子 | http://purl.org/coar/resource_type/c_46ec | |||||
| 資源タイプ | thesis | |||||
| 著者名 |
夏目, 豊彰
× 夏目, 豊彰 |
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| フリガナ |
ナツメ, トヨアキ
× ナツメ, トヨアキ |
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| 著者 |
NATSUME, Toyoaki
× NATSUME, Toyoaki |
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| 学位授与機関 | ||||||
| 学位授与機関名 | 総合研究大学院大学 | |||||
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| 学位名 | 博士（理学） | |||||
| 学位記番号 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | 総研大甲第958号 | |||||
| 研究科 | ||||||
| 値 | 生命科学研究科 | |||||
| 専攻 | ||||||
| 値 | 18 遺伝学専攻 | |||||
| 学位授与年月日 | ||||||
| 学位授与年月日 | 2006-03-24 | |||||
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| 値 | 2005 | |||||
| 要旨 | ||||||
| 内容記述タイプ | Other | |||||
| 内容記述 | Specific chromatin structures on each chromosome location are important for a variety of cellular processes such as transcriptional regulation and chromosome segregation. Although these structures must be precisely maintained during DNA replication to inherit epigenetic information to daughter cells, its underlying mechanisms are poorly understood. In this study, I demonstrate that DNA polymerase α accessory factor, Mcl1, is required for maintaining specific chromatin structures of complex centromere in fission yeast. Fission yeast centromere is composed of two structurally and functionally distinct two chromatin domains. The central domain organizes kinetochore with multiple protein complexes including histone H3 variant, SpCENP-A, and is essential for bipolar attachment to mitotic spindle microtubules from opposite poles. On the other hand, outer repetitive domain forms transcriptionally silent heterochromatin-like structure coated with Heterochromatin Protein 1 (HP1)-homologue, Swi6, and is required for recruiting cohesin complex to tightly bind sister-chromatids. I have shown that Mcl1-deficient cells show alleviation of transcriptional gene silencing of marker genes inserted into both domains. In addition, N-terminal tail of histone H4 is aberrantly acetylated at both domains compared to wild-type strain. At the central domain, SpCENP-A association is abolished in S-phase and the chromatin structure specific to kinetochore is disrupted in Mcl1-deficient cells. At outer repetitive domain, Mcl1 is dispensable for Swi6 loading, suggesting its involvement in an HP1/Swi6-independent pathway for maintaining integrity of heterochromatin. I propose that Mcl1 might maintain histone acetylation pattern suitable for centromeric chromatin structures during DNA replication. This study would provide a novel insight into the close link between DNA replication apparatus and histone acetylation state in the epigenetic inheritance of chromatin structures. | |||||
| 所蔵 | ||||||
| 値 | 有 | |||||
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| 内容記述タイプ | Other | |||||
| 内容記述 | application/pdf | |||||
