TY - JOUR
AU1 - Shi, Xiaobing
AU2 - Hong, Tao
AU3 - Walter, Kay L.
AU4 - Ewalt, Mark
AU5 - Michishita, Eriko
AU6 - Hung, Tiffany
AU7 - Carney, Dylan
AU8 - Peña, Pedro
AU9 - Lan, Fei
AU1 - Kaadige, Mohan R.
AU1 - Lacoste, Nicolas
AU1 - Cayrou, Christelle
AU1 - Davrazou, Foteini
AU1 - Saha, Anjanabha
AU1 - Cairns, Bradley R.
AU1 - Ayer, Donald E.
AU1 - Kutateladze, Tatiana G.
AU1 - Shi, Yang
AU1 - Côté, Jacques
AU2 - Chua, Katrin F.
AU2 - Gozani, Or
AB - Four papers in this issue tackle the hot topic of chromatin remodelling, specifically, how methyl marks on chromatin are 'read' by the proteins that interact with them. Two report on BPTF (bromodomain and PHD domain transcription factor), a subunit of NURF, the nucleosome remodelling factor. It contains a domain known as a PHD finger, which is shown to bind to histone H3 trimethylated at lysine 4 (H3K4) and to maintain proper activity at developmentally critical HOX genes. The accompanying structural study of the complex explains how the site specificity for H3K4 is achieved. The two other papers reveal that the PHD domain of tumour suppressor ING2 also recognizes trimethylated H3K4, and link the histone mark to repression of transcription. The four papers together establish certain PHD finger domains as previously unrecognized chromatin-binding modules. In a News and Views piece, Peter B. Becker discusses what these papers tell us about the function of the chemical modifications of histone tails.
TI - ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression
JF - Nature
DO - 10.1038/nature04835
DA - 2006-05-21
UR - https://www.deepdyve.com/lp/springer-journals/ing2-phd-domain-links-histone-h3-lysine-4-methylation-to-active-gene-8N0waZfqK6
SP - 96
EP - 99
VL - 442
IS - 7098
DP - DeepDyve
ER -