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Spindlin‐1 recognizes methylations of K20 and R23 of histone H4 tail
Author(s) -
Wang Chengliang,
Zhan Li,
Wu Minhao,
Ma Rongsheng,
Yao Jun,
Xiong Ying,
Pan Yang,
Guan Shenheng,
Zhang Xuan,
Zang Jianye
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13281
Subject(s) - histone h4 , chemistry , histone , biochemistry , h3k4me3 , lysine , amino acid , biophysics , biology , dna , gene expression , promoter , gene
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.