In:
FEBS Letters, Wiley, Vol. 591, No. 2 ( 2017-01), p. 425-432
Abstract:
The tumor suppressor inhibitor of growth 4 ( ING 4) regulates chromatin structure by recruiting the histone acetyl transferase complex HBO 1 to sites with histone H3 trimethylated at K4. ING 4 dimerizes through its N‐terminal domain and recognizes H3K4me3 by the C‐terminal plant homeodomain ( PHD ). The central region of ING 4 is disordered and contains the nuclear localization signal. Here, utilizing electrophoresis and nuclear magnetic resonance, we show that ING 4 binds double‐stranded DNA through its central region with micromolar affinity. Our findings suggest that the cooperativity arising from the presence of two DNA ‐binding regions in the ING 4 dimer, as well as two H3K4me3‐binding PHD fingers, may strengthen nucleosome binding and HBO 1 complex recruitment.
Type of Medium:
Online Resource
ISSN:
0014-5793
,
1873-3468
DOI:
10.1002/feb2.2017.591.issue-2
DOI:
10.1002/1873-3468.12514
Language:
English
Publisher:
Wiley
Publication Date:
2017
detail.hit.zdb_id:
1460391-3
SSG:
12
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