5TBN

Solution NMR structure of PHF20 PHD domain in complex with a histone H3K4me2 peptide

5TBN の概要

• エントリーDOI: 10.2210/pdb5tbn/pdb
• NMR情報: BMRB: 30177
• 分子名称: PHD finger protein 20, Histone H3.1, ZINC ION (3 entities in total)
• 機能のキーワード: phd finger, methylated lysine, transcription - structural protein complex, transcription / structural protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8242.01

構造登録者

Cui, G.,Botuyan, M.V.,Mer, G. (登録日: 2016-09-12, 公開日: 2016-10-12, 最終更新日: 2019-12-04)

主引用文献

Klein, B.J.,Wang, X.,Cui, G.,Yuan, C.,Botuyan, M.V.,Lin, K.,Lu, Y.,Wang, X.,Zhao, Y.,Bruns, C.J.,Mer, G.,Shi, X.,Kutateladze, T.G.
PHF20 Readers Link Methylation of Histone H3K4 and p53 with H4K16 Acetylation.
Cell Rep, 17:1158-1170, 2016

PubMed Abstract: PHF20 is a core component of the lysine acetyltransferase complex MOF (male absent on the first)-NSL (non-specific lethal) that generates the major epigenetic mark H4K16ac and is necessary for transcriptional regulation and DNA repair. The role of PHF20 in the complex remains elusive. Here, we report on functional coupling between methylation readers in PHF20. We show that the plant homeodomain (PHD) finger of PHF20 recognizes dimethylated lysine 4 of histone H3 (H3K4me2) and represents an example of a native reader that selects for this modification. Biochemical and structural analyses help to explain this selectivity and the preference of Tudor2, another reader in PHF20, for dimethylated p53. Binding of the PHD finger to H3K4me2 is required for histone acetylation, accumulation of PHF20 at target genes, and transcriptional activation. Together, our findings establish a unique PHF20-mediated link between MOF histone acetyltransferase (HAT), p53, and H3K4me2, and suggest a model for rapid spreading of H4K16ac-enriched open chromatin.

PubMed: 27760318
DOI: 10.1016/j.celrep.2016.09.056

実験手法

SOLUTION NMR