ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression

Xiaobing Shi, Tao Hong, Kay L. Walter, Mark Ewalt, Eriko Michishita, Tiffany Hung, Dylan Carney, Pedro Peña, Fei Lan, Mohan R. Kaadige, Nicolas Lacoste, Christelle Cayrou, Foteini Davrazou, Anjanabha Saha, Bradley R. Cairns, Donald E. Ayer, Tatiana G. Kutateladze, Yang Shi, Jacques Côté, Katrin F. Chua and Or Gozani ()
Additional contact information
Xiaobing Shi: Stanford University
Tao Hong: Stanford University School of Medicine
Kay L. Walter: Stanford University
Mark Ewalt: Stanford University
Eriko Michishita: Stanford University School of Medicine
Tiffany Hung: Stanford University
Dylan Carney: Stanford University
Pedro Peña: University of Colorado Health Sciences Center
Fei Lan: Harvard Medical School
Mohan R. Kaadige: University of Utah
Nicolas Lacoste: Laval University Cancer Research Center
Christelle Cayrou: Laval University Cancer Research Center
Foteini Davrazou: University of Colorado Health Sciences Center
Anjanabha Saha: University of Utah
Bradley R. Cairns: University of Utah
Donald E. Ayer: University of Utah
Tatiana G. Kutateladze: University of Colorado Health Sciences Center
Yang Shi: Harvard Medical School
Jacques Côté: Laval University Cancer Research Center
Katrin F. Chua: Stanford University School of Medicine
Or Gozani: Stanford University

Nature, 2006, vol. 442, issue 7098, 96-99

Abstract: Histones decoded 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.

Date: 2006
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DOI: 10.1038/nature04835

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