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Lysine succinylation on non-histone chromosomal protein HMG-17 (HMGN2) regulates nucleosomal DNA accessibility by disrupting the HMGN2–nucleosome association
RSC Chemical Biology ( IF 4.2 ) Pub Date : 2021-5-27 , DOI: 10.1039/d1cb00070e
Yihang Jing 1 , Gaofei Tian 1 , Xiaoyu Qin 1 , Zheng Liu 1 , Xiang David Li 1
Affiliation  

Lysine succinylation (Ksucc) is a novel posttranslational modification that frequently occurs on chromatin proteins including histones and non-histone proteins. Histone Ksucc affects nucleosome dynamics by increasing the DNA unwrapping rate and accessibility. However, very little is known about the regulation and functions of Ksucc located on non-histone chromosomal proteins. Here, we site-specifically installed a succinyl lysine analogue (Kcsucc) onto the non-histone chromosomal protein HMG-17 (HMGN2) to mimic the natural succinylated protein. We found that the incorporation of Kcsucc into HMGN2 at the K30 site (HMGN2Kc30succ), which is located within the nucleosome-binding domain (NBD), leads to significantly decreased HMGN2 binding to the mononucleosome. HMGN2Kc30succ also increased the nucleosomal DNA accessibility by promoting nucleosomal DNA unwrapping in the entry/exit region. This study reveals a novel mechanism of non-histone protein succinylation on altering chromatin recruitment, which can further affect nucleosome and chromatin dynamics.

中文翻译:

非组蛋白染色体蛋白 HMG-17(HMGN2)上的赖氨酸琥珀酰化通过破坏 HMGN2-核小体关联来调节核小体 DNA 的可及性

赖氨酸琥珀酰化 (Ksucc) 是一种新的翻译后修饰,经常发生在染色质蛋白上,包括组蛋白和非组蛋白。组蛋白 Ksucc 通过增加 DNA 解包率和可及性来影响核小体动力学。然而,关于位于非组蛋白染色体蛋白上的 Ksucc 的调节和功能知之甚少。在这里,我们将琥珀酰赖氨酸类似物 (K c succ)定点安装到非组蛋白染色体蛋白 HMG-17 (HMGN2) 上以模拟天然琥珀酰化蛋白。我们发现 K c succ 在 K30 位点(HMGN2K c30succ),位于核小体结合域 (NBD) 内,导致 HMGN2 与单核小体的结合显着减少。HMGN2K c 30succ 还通过促进核小体 DNA 在进入/退出区域的解缠来增加核小体 DNA 的可及性。这项研究揭示了非组蛋白琥珀酰化改变染色质募集的新机制,这可以进一步影响核小体和染色质动力学。
更新日期:2021-06-15
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