UHRF2 interacts with histone H3K9 acetylation through its PHD domain

Zhang Ting; Zhao Linglin; Zeng Shengyuan; Duan Changzhu

doi:10.13406/j.cnki.cyxb.000635

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UHRF2 interacts with histone H3K9 acetylation through its PHD domain

更新时间：2024-01-17

- UHRF2 interacts with histone H3K9 acetylation through its PHD domain
- Journal of Chongqing Medical University Vol. 40, Issue 11, Pages: 1485-1490(2015)
- 作者机构：
  
  重庆医科大学基础医学院细胞生物学遗传学教研室
- 作者简介：
- 基金信息：
- DOI：10.13406/j.cnki.cyxb.000635
  CLC： R735.7
- Published：2015，
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[1]张婷,赵灵琳,曾盛源,段昌柱.UHRF2通过其PHD结构域与组蛋白H3K9乙酰化相互作用[J].重庆医科大学学报,2015,40(11):1485-1490.

Zhang Ting, Zhao Linglin, Zeng Shengyuan, et al. UHRF2 interacts with histone H3K9 acetylation through its PHD domain. [J]. Journal of Chongqing Medical University 40(11):1485-1490(2015)
[1]张婷,赵灵琳,曾盛源,段昌柱.UHRF2通过其PHD结构域与组蛋白H3K9乙酰化相互作用[J].重庆医科大学学报,2015,40(11):1485-1490. DOI： 10.13406/j.cnki.cyxb.000635.

Zhang Ting, Zhao Linglin, Zeng Shengyuan, et al. UHRF2 interacts with histone H3K9 acetylation through its PHD domain. [J]. Journal of Chongqing Medical University 40(11):1485-1490(2015) DOI： 10.13406/j.cnki.cyxb.000635.

摘要

目的:探讨UHRF2蛋白与组蛋白组蛋白H3第9位赖氨酸残基乙酰化（Histone H3 Lys9 acetylation

H3K9ac）的相互作用及两者相互作用结合区域的测定。方法:在LO2和Hep G2细胞中转染p CMV-FLAG-UHRF2

激光共聚焦分别检测UHRF2与组蛋白H3、H3K9ac和H3K14ac在细胞内的共定位。采用免疫沉淀技术分别检测UHRF2与组蛋白H3、H3K9ac和组蛋白H3第14位赖氨酸基乙酰化（Histone H3 Lys14 acetylation

H3K14ac）在细胞中的相互作用

以及用UHRF2的不同缺失体层粒分别与组蛋白H3K9ac相结合方法来检测UHRF2与之相互作用的功能性结合区域。结果:（1）UHRF2与组蛋白H3、H3K9ac和H3K14ac在LO2和Hep G2细胞中存在共定位现象。（2）在LO2和Hep G2细胞中

UHRF2与H3K9ac相互结合。（3）在正常肝细胞LO2中

UHRF2与H3K9ac相互作用的结合区域为PHD结构域。而在肝癌细胞Hep G2中

除了PHD结构域以外

YDG/SRA结构域也是UHRF2与H3K9ac的关键结构域。结论:UHRF2通过其PHD结构域与H3K9ac相互作用。

Abstract

Objective:To investigate the association of ubiquitin-like with PHD and ring finger domains 2(UHRF2)with histone H3Lys9 acetylation(H3K9ac)and to find the required domain for UHRF2 interacting with H3K9 ac. Methods:LO2 and Hep G2 cells were transfected with p CMV-FLAG-UHRF2 to observe the colocation between UHRF2 and histone H3(H3)

H3K9 ac

histone H3 Lys14acetylation(H3K14ac) by immunofluorescence assay and laser scanning confocal microscopy. The interaction between UHRF2 and H3

H3K9 ac

H3K14ac in LO2 and Hep G2 cells were detected by immunoprecipitation. Then

LO2 and Hep G2 cells were transfected with deletion mutants of UHRF2 to test the functional binding region for UHRF2 interacting with H3K9 ac. Results:(1)UHRF2 colocalized with H3

H3K9 ac and H3K14 ac in LO2 and Hep G2 cells.(2)UHRF2 interacted with H3K9 ac in LO2 and Hep G2 cells.(3)In LO2 cells

PHD domain was the key domain for UHRF2 to interact with H3K9 ac

while in Hep G2 cancer cells

not only PHD domain but also YDG/SRA domain was the functional binding region for UHRF2 interacting with H3K9 ac. Conclusion:UHRF2 interacts with H3K9 ac through its PHD domain.

关键词

UHRF2组蛋白H3组蛋白H3K9乙酰化组蛋白H3K14乙酰化表观遗传学

Keywords

ubiquitin-like with PHD and ring finger domains 2histone H3histone H3 Lys9 acetylationhistone H3 Lys14 acetylationepigenetics

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Related Author

Xu Jing

Related Institution

Department of Neurology, Tianjin Medical University General Hospital

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