The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide.

The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide.
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DOI:
10.1002/prot.22140
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发表时间:
2008-09
期刊:
影响因子:
2.9
通讯作者:
Kutateladze TG
Kutateladze TG
中科院分区:
生物学4区
文献类型:
--
作者:
Champagne KS;Saksouk N;Peña PV;Johnson K;Ullah M;Yang XJ;Côté J;Kutateladze TG

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Chromatin dynamics regulates diverse nuclear processes and influences cellular viability and tumorigenesis. The discrete chromatin states are linked to covalent histone modifications that control the extent of DNA accessibility to transacting factors. One of the most common epigenetic modifications is methylation of histone H3 at lysine 4 (H3K4). Lys4 can be mono-, di-, or tri-methylated, and the tri-methylated mark (H3K4me3) is normally associated with euchromatin and active gene transcription. 1, 2The inhibitor of growth (ING) family of tumor suppressors contain a C-terminal plant homeodomain (PHD) finger. This conserved zinc-binding module is found in many nuclear proteins including transcription factors, histone modifying enzymes, and ATP dependent chromatin remodeling complexes. 3-5 A subset of PHD fingers has recently been shown to bind methylated and unmodified histone tails, 5-9 with the H3K4me3 mark being specifically recognized by ING proteins. Unlike ING1 and ING2, which have been identified as components of histone deacetylase (HDAC) complexes, ING5 associates with histone acetyltransferase (HAT) complexes containing MOZ (monocytic leukemia zinc finger protein)/MORF (MOZ-related factor) and HBO1. 10
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