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2
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Specific recognition of phosphorylated tail of H2AX by the tandem BRCT domains of MCPH1 revealed by complex structure.通过复合物结构揭示了 MCPH1 串联 BRCT 结构域对 H2AX 磷酸化尾巴的特异性识别。
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DNA 损伤反应蛋白 MCPH1 对组蛋白变体 H2A.X 上磷酸丝氨酸和磷酸苏氨酸的双重识别。

Dual recognition of phosphoserine and phosphotyrosine in histone variant H2A.X by DNA damage response protein MCPH1.

机构信息

Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA.

出版信息

Proc Natl Acad Sci U S A. 2012 Sep 4;109(36):14381-6. doi: 10.1073/pnas.1212366109. Epub 2012 Aug 20.

DOI:10.1073/pnas.1212366109
PMID:22908299
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3437875/
Abstract

Tyr142, the C-terminal amino acid of histone variant H2A.X is phosphorylated by WSTF (Williams-Beuren syndrome transcription factor), a component of the WICH complex (WSTF-ISWI chromatin-remodeling complex), under basal conditions in the cell. In response to DNA double-strand breaks (DSBs), H2A.X is instantaneously phosphorylated at Ser139 by the kinases ATM and ATR and is progressively dephosphorylated at Tyr142 by the Eya1 and Eya3 tyrosine phosphatases, resulting in a temporal switch from a postulated diphosphorylated (pSer139, pTyr142) to monophosphorylated (pSer139) H2A.X state. How mediator proteins interpret these two signals remains a question of fundamental interest. We provide structural, biochemical, and cellular evidence that Microcephalin (MCPH1), an early DNA damage response protein, can read both modifications via its tandem BRCA1 C-terminal (BRCT) domains, thereby emerging as a versatile sensor of H2A.X phosphorylation marks. We show that MCPH1 recruitment to sites of DNA damage is linked to both states of H2A.X.

摘要

Tyr142 是组蛋白变体 H2A.X 的 C 末端氨基酸，在细胞的基础条件下，可被 WICH 复合物（WSTF-ISWI 染色质重塑复合物）的组成部分 WSTF（威廉姆斯-比伦综合征转录因子）磷酸化。在 DNA 双链断裂（DSBs）的情况下，H2A.X 可被 ATM 和 ATR 激酶立即磷酸化 Ser139，并被 Eya1 和 Eya3 酪氨酸磷酸酶逐步去磷酸化 Tyr142，导致从假定的双磷酸化（pSer139，pTyr142）状态到单磷酸化（pSer139）状态的时间开关。中介蛋白如何解释这两个信号仍然是一个具有根本意义的问题。我们提供了结构、生化和细胞证据，表明 Microcephalin（MCPH1），一种早期的 DNA 损伤反应蛋白，可以通过其串联 BRCA1 C 末端（BRCT）结构域读取这两种修饰，从而成为 H2A.X 磷酸化标记的多功能传感器。我们表明，MCPH1 募集到 DNA 损伤部位与 H2A.X 的两种状态有关。