Letter

Nature advance online publication 21 May 2006 | = doi:10.1038/nature04835; = Received 27=20 February 2006; Accepted 17 April 2006; Published online 21 May 2006

ING2 PHD domain links histone H3 lysine 4 methylation to = active gene=20 repression

Xiaobing Shi¹,=20 Tao Hong²,=20 Kay L. Walter¹,=20 Mark Ewalt¹,=20 Eriko Michishita²,=20 Tiffany Hung¹,=20 Dylan Carney¹,=20 Pedro Pe=F1a³,=20 Fei Lan⁴,=20 Mohan R. Kaadige⁵,=20 Nicolas Lacoste⁶,=20 Christelle Cayrou⁶,=20 Foteini Davrazou³,=20 Anjanabha Saha⁵,=20 Bradley R. Cairns⁵,=20 Donald E. Ayer⁵,=20 Tatiana G. Kutateladze³,=20 Yang Shi⁴,=20 Jacques C=F4t=E9⁶,=20 Katrin F. Chua^2,⁷=20 and Or Gozani¹

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Dynamic regulation of diverse nuclear processes is = intimately=20 linked to covalent modifications of chromatin^1,². = Much=20 attention has focused on methylation at lysine 4 of histone H3 (H3K4), = owing to=20 its association with euchromatic genomic regions^{3, =}⁴. H3K4=20 can be mono-, di- or tri-methylated. Trimethylated H3K4 (H3K4me3) is=20 preferentially detected at active genes, and is proposed to promote gene = expression through recognition by transcription-activating effector=20 molecules⁵. Here we identify a novel class of methylated H3K4 = effector domains=97the PHD domains of the ING (for inhibitor of growth) = family of=20 tumour suppressor proteins. The ING PHD domains are specific and highly = robust=20 binding modules for H3K4me3 and H3K4me2. ING2, a native subunit of a = repressive=20 mSin3a=96HDAC1 histone deacetylase complex⁶, binds with high = affinity=20 to the trimethylated species. In response to DNA damage, recognition of = H3K4me3=20 by the ING2 PHD domain stabilizes the mSin3a=96HDAC1 complex at the = promoters of=20 proliferation genes. This pathway constitutes a new mechanism by which = H3K4me3=20 functions in active gene repression. Furthermore, ING2 modulates = cellular=20 responses to genotoxic insults, and these functions are critically = dependent on=20 ING2 interaction with H3K4me3. Together, our findings establish a = pivotal role=20 for trimethylation of H3K4 in gene repression and, potentially, tumour=20 suppressor mechanisms.

Department of Biological Sciences, Stanford University, = and
Department of Medicine, Stanford University School of = Medicine,=20 Stanford, California 94305, USA=20
Department of Pharmacology, University of Colorado Health = Sciences=20 Center, Aurora, Colorado 80045, USA=20
Department of Pathology, Harvard Medical School, Boston,=20 Massachusetts 02115, USA=20
Huntsman Cancer Institute and Department of Oncological = Sciences,=20 University of Utah, Salt Lake City, Utah 84112, USA=20
Laval University Cancer Research Center, Quebec City, = Quebec G1R=20 2J6, Canada=20
Geriatric Research, Education and Clinical Center, VA Palo = Alto=20 Health Care System, Palo Alto, California 94304, USA

Correspondence to: Or Gozani¹=20 Correspondence and requests for materials should be addressed to O.G.=20 (Email: ogozani@stanford.edu).

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Letter

ING2 PHD domain links histone H3 lysine 4 methylation to = active gene=20 repression

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