H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation.
H2B ubiquitination recruits FACT to maintain a stable altered nucleosome state for transcriptional activation.
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H2B 泛素化招募 FACT 来维持转录激活的稳定改变的核小体状态
DOI：
10.1038/s41467-023-36467-3
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发表时间：
2023-02-10
影响因子：
16.6
通讯作者：
Chen, Ping
中科院分区：
文献类型：
--
作者：
Luo, Anfeng;Kong, Jingwei;Chen, Jun;Xiao, Xue;Lan, Jie;Li, Xiaorong;Liu, Cuifang;Wang, Peng-Ye;Li, Guohong;Li, Wei;Chen, Ping
研究发现，组蛋白H2B赖氨酸120位点的单泛素化（ubH2B）通过与组蛋白伴侣FACT（促进染色质转录）协同调节转录伸长，并在基于染色质的转录过程中发挥重要作用。然而，ubH2B如何在核小体水平上与FACT直接合作的机制仍然是未知的。在这项研究中，我们证明了ubH2B损害核小体的机械稳定性，并通过增强FACT在核小体上的结合来帮助招募FACT。FACT倾向于结合和沉积H2A-ubH2B二聚体以形成完整的核小体。值得注意的是，FACT与ubh2b -核小体的良好结合极大地增强了核小体的稳定性并保持了其完整性。全基因组和时间序列ChIP-qPCR分析显示，ubH2B和FACT获得的核小体稳定改变状态为基因转录提供了关键平台。我们的研究结果为ubH2B如何直接与FACT合作调节基因转录的核小体动力学提供了机制见解。在这里，作者在核小体水平上研究了泛素化组蛋白H2B （ubH2B）与FACT之间的直接合作。他们发现ubH2B增强了FACT的伴侣特性，招募FACT形成稳定的核小体状态，并为转录提供了一个关键平台。
Histone H2B mono-ubiquitination at lysine 120 (ubH2B) has been found to regulate transcriptional elongation by collaborating with the histone chaperone FACT (Facilitates Chromatin Transcription) and plays essential roles in chromatin-based transcriptional processes. However, the mechanism of how ubH2B directly collaborates with FACT at the nucleosome level still remains elusive. In this study, we demonstrate that ubH2B impairs the mechanical stability of the nucleosome and helps to recruit FACT by enhancing the binding of FACT on the nucleosome. FACT prefers to bind and deposit H2A-ubH2B dimers to form an intact nucleosome. Strikingly, the preferable binding of FACT on ubH2B-nucleosome greatly enhances nucleosome stability and maintains its integrity. The stable altered nucleosome state obtained by ubH2B and FACT provides a key platform for gene transcription, as revealed by genome-wide and time-course ChIP-qPCR analyses. Our findings provide mechanistic insights of how ubH2B directly collaborates with FACT to regulate nucleosome dynamics for gene transcription. Here the authors investigated the direct collaboration between ubiquitinated histone H2B (ubH2B) with FACT at the nucleosome level. They found ubH2B enhances FACT’s chaperone property, recruits FACT to form a stable altered nucleosome state, and provides a key platform for transcription.
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