A PHD finger of NURF couples histone H3 lysine 4 trimethylation with chromatin remodelling

Joanna Wysocka, Tomek Swigut, Hua Xiao, Thomas A. Milne, So Yeon Kwon, Joe Landry, Monika Kauer, Alan J. Tackett, Brian T. Chait, Paul Badenhorst, Carl Wu () and C. David Allis ()
Additional contact information
Joanna Wysocka: Laboratory of Chromatin Biology
Tomek Swigut: Laboratory of Molecular Vertebrate Embryology
Hua Xiao: National Cancer Institute, NIH
Thomas A. Milne: Laboratory of Chromatin Biology
So Yeon Kwon: University of Birmingham
Joe Landry: National Cancer Institute, NIH
Monika Kauer: Laboratory of Chromatin Biology
Alan J. Tackett: The Rockefeller University
Brian T. Chait: The Rockefeller University
Paul Badenhorst: University of Birmingham
Carl Wu: National Cancer Institute, NIH
C. David Allis: Laboratory of Chromatin Biology

Nature, 2006, vol. 442, issue 7098, 86-90

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/nature04815

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