Publication Date:
2018
Description:
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.
Print ISSN:
0014-5793
Electronic ISSN:
1873-3468
Topics:
Biology
,
Chemistry and Pharmacology
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