Comprehensive analysis of dynamics of histone H4 acetylation in mitotic barley cells

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Nucleosomal histones are covalently modified at specific amino acid residues. In the case of histone H4, four lysines (K5, K8, K12, and K16) are acetylated. In the current studies, we examined the dynamics of histone H4 acetylation at K8 and K12 in mitotic barley cells using a three-dimensional immunofluorescent method. Based on the results and previous studies on the dynamics of K5 and K16 acetylation, we provide a comprehensive view of the dynamics of H4 acetylation. Interphase nuclei exhibit strong acetylation in the centromeric region at K5, K8 and K12. In the case of K12, strong acetylation at nucleolar organizing regions was observed from prophase to anaphase. The dynamics of K12 were closely related to those of K5. On the other hand, K8 exhibited a pattern of almost uniform acetylation from prophase to telophase and strong acetylation in distal regions of chromosomes at both metaphase and anaphase, which is very similar to the dynamics of K16 acetylation. Thus, it appears that there is pair-wise acetylation of K12 and K5 in the nucleolar organizing regions and of K8 and K16 in the gene-rich regions. Together, these results suggest that pair-wise dynamics of H4 acetylation regulate chromosomal structure and function during the cell cycle.<br>

収録刊行物

  • Genes & genetic systems  

    Genes & genetic systems 80(4), 269-276, 2005-08-25 

    The Genetics Society of Japan

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各種コード

  • NII論文ID(NAID)
    10018280175
  • NII書誌ID(NCID)
    AA11077421
  • 本文言語コード
    ENG
  • 資料種別
    ART
  • ISSN
    13417568
  • NDL 記事登録ID
    7681524
  • NDL 雑誌分類
    ZR1(科学技術--生物学)
  • NDL 請求記号
    Z53-W539
  • データ提供元
    CJP書誌  CJP引用  NDL  J-STAGE 
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