Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail
Spindlin-1 recognizes methylations of K20 and R23 of histone H4 tail
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Spindlin-1 识别组蛋白 H4 尾部 K20 和 R23 的甲基化
DOI：
10.1002/1873-3468.13281
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发表时间：
2018
期刊：
影响因子：
3.5
通讯作者：
Zang Jianye
中科院分区：
文献类型：
--
作者：
Wang Chengliang;Zhan Li;Wu Minhao;Ma Rongsheng;Yao Jun;Xiong Ying;Pan Yang;Guan Shenheng;Zhang Xuan;Zang Jianye
使用结合交联、下拉分析和通过细胞培养物中的氨基酸进行稳定同位素标记与质谱的方法，我们确定了含有Tudor结构域的蛋白质Spindlin-1识别组蛋白H4赖氨酸20（H4 K20 me 3）的三甲基化。Spindlin-1与H4 K20 me 3的结合亲和力弱于与H3 K4 me 3的结合亲和力，表明H4 K20 me 3是Spindlin-1的第二底物。Spindlin-1与H4 K20 me 3肽复合物的结构研究表明，Spindlin-1获得了H4 K20 me 3识别的独特结合模式。进一步的生化分析发现，Spindlin-1也结合H4的甲基化R23，为Spindlin-1的功能提供了新的线索。
Using methods combining cross‐linking, pull‐down assays, and stable isotope labeling by amino acids in cell culture with mass spectrometry, we identified that the Tudor domain‐containing protein Spindlin‐1 recognizes trimethylation of histone H4 lysine 20 (H4K20me3). The binding affinity of Spindlin‐1 to H4K20me3 is weaker than that to H3K4me3, indicating H4K20me3 as a secondary substrate for Spindlin‐1. Structural studies of Spindlin‐1 in complex with the H4K20me3 peptide indicate that Spindlin‐1 attains a distinct binding mode for H4K20me3 recognition. Further biochemical analysis identified that Spindlin‐1 also binds methylated R23 of H4, providing new clues for the function of Spindlin‐1.