In:
FEBS Letters, Wiley, Vol. 592, No. 24 ( 2018-12), p. 4098-4110
Abstract:
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.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/feb2.2018.592.issue-24
DOI:
10.1002/1873-3468.13281
Language:
English
Publisher:
Wiley
Publication Date:
2018
detail.hit.zdb_id:
1460391-3
SSG:
12
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