DisorderING promotes epigenetic order

Tallen, Gesche; Riabowol, Karl

doi:10.1002/1873-3468.12552

Cited by 3 publications

(1 citation statement)

References 16 publications

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“…The actual ligand of ING4 is the nucleosome, consisting of a histone octamer with two copies of histone H3 and a 147 bp-long DNA duplex. Therefore, the overall affinity will even higher because of two cooperative effects: the micromolar affinity binding of the central region of ING4 to DNA and the presence of two histone H3 N-terminal tails in each nucleosome [23]. ING4 does not work alone but as member of the histone acetyl transferase HBO1 complex, which includes the JADE proteins with PHD fingers that also bind to histone H3 N-terminal tail [24].…”

Section: Discussionmentioning

confidence: 99%

Macromolecular Crowding Increases the Affinity of the PHD of ING4 for the Histone H3K4me3 Mark

Palacios

Blanco

2020

Biomolecules

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The five members of the family of tumor suppressors ING contain a Plant Homeodomain (PHD) that specifically recognizes histone H3 trimethylated at lysine 4 (H3K4me3) with an affinity in the low micromolar range. Here, we use NMR to show that in the presence of 15% Ficoll 70, an inert macromolecular crowding agent, the mode of binding does not change but the affinity increases by one order of magnitude. The affinity increases also for unmethylated histone H3 tail, but the difference with H3K4me3 is larger in the presence of Ficoll. These results indicate that in the cellular milieu, the affinity of the ING proteins for their chromatin target is larger than previously thought.

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Section: Discussionmentioning

confidence: 99%