Letter

Nature advance online publication 21 May 2006 | = doi:10.1038/nature04814; = Received 27=20 February 2006; Accepted 11 April 2006; Published online 21 May 2006

Molecular mechanism of histone H3K4me3 recognition by plant = homeodomain of ING2

Pedro V. Pe=F1a¹,=20 Foteini Davrazou¹,=20 Xiaobing Shi³,=20 Kay L. Walter³,=20 Vladislav V. Verkhusha⁴,=20 Or Gozani³,=20 Rui Zhao²=20 and Tatiana G. Kutateladze¹

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Covalent modifications of histone tails have a key role = in=20 regulating chromatin structure and controlling transcriptional activity. = In=20 eukaryotes, histone H3 trimethylated at lysine 4 (H3K4me3) is associated = with=20 active chromatin and gene expression^1,^2,^3,=20⁴. We recently found that plant homeodomain (PHD) = finger of=20 tumour suppressor ING2 (inhibitor of growth 2) binds H3K4me3 and = represents a=20 new family of modules that target this epigenetic mark⁵. The=20 molecular mechanism of H3K4me3 recognition, however, remains unknown. = Here we=20 report a 2.0 =C5 resolution structure of the mouse ING2 PHD finger = in complex=20 with a histone H3 peptide trimethylated at lysine 4. The H3K4me3 tail is = bound=20 in an extended conformation in a deep and extensive binding site = consisting of=20 elements that are conserved among the ING family of proteins. The=20 trimethylammonium group of Lys 4 is recognized by the aromatic side = chains of=20 Y215 and W238 residues, whereas the intermolecular hydrogen-bonding and=20 complementary surface interactions, involving Ala 1, Arg 2, = Thr 3=20 and Thr 6 of the peptide, account for the PHD finger's high = specificity and=20 affinity. Substitution of the binding site residues disrupts H3K4me3 = interaction=20 in vitro and impairs the ability of ING2 to induce apoptosis = in=20 vivo. Strong binding of other ING and YNG PHD fingers suggests that = the=20 recognition of H3K4me3 histone code is a general feature of the ING/YNG=20 proteins. Elucidation of the mechanisms underlying this novel function = of PHD=20 fingers provides a basis for deciphering the role of the ING family of = tumour=20 suppressors in chromatin regulation and signalling.

Department of Pharmacology, and
Department of Biochemistry and Molecular Genetics, = University of=20 Colorado Health Sciences Center, Aurora, Colorado 80045, USA=20
Department of Biological Sciences, Stanford University, = Stanford,=20 California 94305, USA=20
Department of Anatomy and Structural Biology, Albert = Einstein=20 College of Medicine, Bronx, New York 10461, USA

Correspondence to: Tatiana G. Kutateladze¹=20 Correspondence and requests for materials should be addressed to T.G.K.=20 (Email: Tatiana.Kutateladze@uchsc.e= du).The=20 coordinates have been deposited in the Protein Data Bank under accession = number=20 2G6Q.

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=A9 2006 = Nature=20 Publishing Group =96 partner of AGORA, HINARI, = Cross Ref and COUNTER =

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Molecular mechanism of histone H3K4me3 recognition by plant = homeodomain of ING2

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