Premium
The tumor suppressor inhibitor of growth 4 binds double‐stranded DNA through its disordered central region
Author(s) -
Ormaza Georgina,
Medagli Barbara,
Ibáñez de Opakua Alain,
Rodríguez Jhon A.,
Merino Nekane,
Villate Maider,
Onesti Silvia,
Blanco Francisco J.
Publication year - 2017
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 - 10.1002/1873-3468.12514
Subject(s) - nucleosome , cooperative binding , chromatin , dna , chemistry , histone , microbiology and biotechnology , binding site , h3k4me3 , cooperativity , biophysics , biology , biochemistry , gene , gene expression , promoter
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.