• 其他栏目

    宋晓元

    • 教授 博士生导师 硕士生导师
    • 教师英文名称:Xiaoyuan Song
    • 教师拼音名称:songxiaoyuan
    • 电子邮箱:
    • 学历:博士研究生毕业
    • 办公地点:中国科学技术大学西校区科技东楼915
    • 学位:博士
    • 毕业院校:美国罗彻斯特大学
    • 学科:生物学
    • 2022-10-01曾获荣誉当选:“典赞 2022科普安徽”科普活动“年度科普作品”
    • 2021-05-01曾获荣誉当选:安徽省优秀科普作品一等奖
    • 2019-09-16曾获荣誉当选:王宽诚育才奖

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    The nonhistone, N-terminal tail of an essential, chimeric H2A variant regulates mitotic H3-S10 dephosphorylation.

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    DOI码:10.1101/gad.182683.111

    发表刊物:Genes & Development

    摘要:H2A.Y is an essential, divergent Tetrahymena thermophila histone variant. It has a long nonhistone N terminus that contains leucine-rich repeats (LRR) and an LRR cap domain with similarity to Sds22p, a regulator of yeast protein phosphatase 1 (PP1) activity in the nucleus. In growing cells, H2A.Y is incorporated into micronuclei only during S phase, which occurs immediately after micronuclear mitosis. Depletion of H2A.Y causes prolonged retention of mitosis-associated histone H3-S10 phosphorylation and mitotic abnormalities that mimic S10E mutation. In cells where H2A.Y is depleted, an inducible chimeric gene, in which the H2A.Y N terminus is attached to H2A.X, is shown to regulate micronuclear H3-S10 phosphorylation. H2A.Y can also be specifically coimmunoprecipitated with a Tetrahymena PP1 ortholog (Ppo1p). Taken together, these results argue that the N terminus of H2A.Y functions to regulate H3-S10 dephosphorylation. This striking in vivo case of "cross-talk" between a H2A variant and a specific post-translational modification of another histone demonstrates a novel function for a histone variant.

    卷号:26

    期号:6

    页面范围:615-29

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