From: Subject: ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression : Nature Date: Tue, 23 May 2006 13:49:55 +0200 MIME-Version: 1.0 Content-Type: multipart/related; type="text/html"; boundary="----=_NextPart_000_0033_01C67E6F.C6215260" X-MimeOLE: Produced By Microsoft MimeOLE V6.00.2900.2869 This is a multi-part message in MIME format. ------=_NextPart_000_0033_01C67E6F.C6215260 Content-Type: text/html; charset="iso-8859-1" Content-Transfer-Encoding: quoted-printable Content-Location: http://www.nature.com/nature/journal/vaop/ncurrent/full/nature04835.html ING2 PHD domain = links histone H3 lysine 4 methylation to active gene repression : = Nature
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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. Chua2,7=20 and Or Gozani1

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Abstract

Dynamic regulation of diverse nuclear processes is = intimately=20 linked to covalent modifications of chromatin1,=20 2.=20 Much attention has focused on methylation at lysine 4 of histone H3 = (H3K4),=20 owing to its association with euchromatic genomic regions3,=20 4.=20 H3K4 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.=20 Here we identify a novel class of methylated H3K4 effector domains=97the = PHD=20 domains of the ING (for inhibitor of growth) family of tumour suppressor = proteins. The ING PHD domains are specific and highly robust binding = modules for=20 H3K4me3 and H3K4me2. ING2, a native subunit of a repressive = mSin3a=96HDAC1 histone=20 deacetylase complex6,=20 binds with high affinity to the trimethylated species. In response to = DNA=20 damage, recognition of H3K4me3 by the ING2 PHD domain stabilizes the=20 mSin3a=96HDAC1 complex at the promoters of proliferation genes. This = pathway=20 constitutes a new mechanism by which H3K4me3 functions in active gene=20 repression. Furthermore, ING2 modulates cellular responses to genotoxic = insults,=20 and these functions are critically dependent on ING2 interaction with = H3K4me3.=20 Together, our findings establish a pivotal role for trimethylation of = H3K4 in=20 gene repression and, potentially, tumour suppressor = mechanisms.

Binding of the ING2 PHD (ING2PHD) domain to = the lipid=20 signalling molecule phosphatidylinositol-5-phosphate (PtdIns(5)P) is = critical=20 for ING2 recruitment to chromatin during DNA damage responses7.=20 Because some phosphatidylinositol phosphate (PtdInsP)-binding domains = function=20 through dual recognition of lipids and peptides8,=20 9,=20 we asked whether the ING2 PHD domain has protein, in addition to = PtdInsP,=20 ligands. In an in vitro pull-down screen for ING2PHD = protein=20 binding partners, we identified histone H3 (Supplementary=20 Fig. S1a). ING2PHD-binding to H3 was independent of=20 PtdIns(5)P-binding, and was confirmed in direct pull-down assays from = purified=20 bulk histones (Fig.=20 1a, c;=20 Supplementary=20 Fig. S1a).

Figure=20 1: The ING2 PHD domain specifically binds to H3K4me3 in=20 vitro.

a, Coomassie-blue stain of glutathione = S-transferase=20 (GST)=96ING2PHD and GST control pull downs from calf thymus = histones.=20 b, Gel shift showing ING2PHD-binding to purified = native=20 nucleosomes. Ethidium-bromide stain of nucleosomal DNA on a = non-denaturing gel.=20 c, Western blot analysis of GST pull-down assays as in a.=20 d, The ING2 PHD domain preferentially binds H3K4me3 peptides. = Western=20 analysis of histone peptide pull downs with the indicated GST fusion = proteins=20 and biotinylated peptides. Peptide integrity was confirmed with known=20 methyl-lysine-binding domains (Supplementary Fig. S1d, e). aa, amino = acids.=20 e, Methylation at H3K4 is required for ING2PHD-binding = to=20 chromatin in vitro. Western analysis of GST=96ING2PHD = pull-down=20 assays of chromatin purified from wild-type or Set1-null S. = cerevisiae=20 strains. f, PHD domains of yeast and human ING family proteins=20 preferentially bind to H3K4me2/3 in histone peptide binding = assays.

High=20 resolution image and legend (47K)

The ING2 PHD domain bound robustly to native = mononucleosomes=20 purified from mammalian cells (Fig.=20 1b), but, in contrast to the ACF (ATP-dependent chromatin-assembly = factor)=20 and p300 (E1A binding protein p300) PHD domains, did not bind = mononucleosomes=20 reconstituted from recombinant histones (Supplementary=20 Fig. S1b)10,=20 11.=20 Therefore, we postulated that this domain might recognize a = post-translational=20 H3 modification. Western blot analysis of ING2PHD-bound = histones=20 revealed significant methylation of H3 on lysine 4, but not lysine 9 (Fig.=20 1c). In in vitro binding assays of methylated histone = peptides, the=20 ING2 PHD domain bound most strongly to H3K4me3, with lower affinity to = H3K4me2,=20 and not at all to numerous other peptides (Fig.=20 1d; Supplementary=20 Fig. S1c).

In the accompanying paper describing the crystal = structure of the=20 ING2PHD=96H3K4me3 peptide complex, aspartate 230 (D230) of = ING2 is=20 implicated in H3K4me3 recognition12.=20 Accordingly, substitution of D230 to alanine (ING2PHD-D230A) = mostly=20 abolished H3K4me3 peptide binding (Fig.=20 1d). The effect of this substitution is not due to unfolding of the = PHD=20 domain, as determined by NMR two-dimensional spectra12.=20 Notably, this mutation has no effect on the lipid-binding activity of = the ING2=20 PHD domain (Supplementary=20 Fig. S2), and therefore allows selective abrogation of the = ING2=96H3K4me3=20 interaction for functional studies (see below). Finally, full-length = ING2, but=20 not a PHD domain deletion mutant (ING23DDelta=20PHD), bound specifically to methylated = H3K4 peptides=20 (Fig.=20 1d). Thus, the ING2 PHD domain is necessary and sufficient for ING2=20 interaction with H3K4me3 in vitro.

The association of the ING2 PHD domain with H3 was = increased by=20 hypermethylation of bulk histones with the H3K4 methyltransferase SET7 = (also=20 known as SET9; ref. 13)=20 and decreased by the H3K4 demethylase LSD1 (also known as AOF2; ref. 14)=20 (Supplementary=20 Fig. S3). Moreover, the ING2 PHD domain bound efficiently to H3 in = chromatin=20 purified from wild-type Saccharomyces cerevisiae strains, but not = from=20 strains lacking the H3K4 methyltransferase Set1 (Fig.=20 1e). Together, these data indicate that H3K4 methylation is critical = for=20 ING2PHD-binding to histone H3 at chromatin in = vitro.

Like the ING2 PHD domain, the PHD domains of the S.=20 cerevisiae and other human ING family members all bound = preferentially to=20 di- and tri-methylated H3K4, whereas that of the Mi3Dalpha=202 autoantigen bound to trimethylated H3K36 (Fig.=20 1f; Supplementary=20 Fig. S4a, b). Thus, recognition of methylated histone peptides is a = general=20 feature of at least a subset of PHD domains, with the ING PHD family=20 constituting a novel class of binding modules for methylated H3K4.

The functional role of ING2 in the context of = mSin3a=96HDAC1=20 complexes is unclear6.=20 We postulated that ING2 bridges the mSin3a=96HDAC1 complex with = methylated H3K4=20 through its PHD domain, and thereby promotes deacetylation of nearby = acetylated=20 histone residues. To test this idea, we purified ING2=96mSin3a=96HDAC1 = complexes=20 containing ING2, ING23DDelta=20PHD or ING2D230A. Neither = mutation=20 altered the composition of the ING2 complexes (Fig.=20 2a; Supplementary=20 Fig. S5). In peptide pull-down assays, the wild-type, but not = mutant, ING2=20 complexes bound preferentially to H3K4me3 (Fig.=20 2b). Furthermore, hypermethylation of H3K4 by SET7 enhanced the = histone=20 deacetylase activity of the wild-type, but not mutant, ING2 complexes = (Figs=20 2c, d).=20 Therefore, recognition of methylated H3K4 by the ING2 PHD domain = promotes the=20 histone deacetylase activity of mSin3a=96HDAC1 complexes in = vitro.

Figure=20 2: Methylated H3K4 recognition by the ING2 PHD domain enhances=20 ING2-associated HDAC1 histone deacetylase activity in=20 vitro.

a, Western analysis of affinity-purified wild-type = and mutant=20 Flag=96ING2 complexes. Mock, empty vector control immunoprecipitation. = b,=20 Binding of ING2 complexes to methylated H3K4 peptides requires an intact = PHD=20 domain. Anti-ING2 western analysis of histone peptide pull downs from = the=20 indicated HDAC1=96ING2 complexes. c, Histone deacetylation by = HDAC1 in=20 wild-type, but not mutant, ING2 complexes is increased by binding of the = ING2=20 PHD domain to methylated H3K4. Western analysis of in vitro = histone=20 deacetylation reactions by ING2 complexes in the presence or absence of=20 methylation by SET7. Histone deacetylase inhibition with trichostatin A = (TSA) is=20 shown as a control. d, Quantification of relative histone = deacetylase=20 activity of ING2 complexes as in c from three independent = experiments.=20 Error bars indicate the s.e.m.

High=20 resolution image and legend (54K)

We next studied the recognition of methylated H3K4 by = the ING2 PHD=20 domain in the context of physiological chromatin in cells. In = protein=96protein=20 chromatin immunoprecipitation (ChIP) assays15,=20 wild-type ING2 associated strongly with H3K4me3, but only weakly with = H3K4me2=20 and not at all with other modified histones, suggesting that H3K4me3 is = the=20 preferred in vivo target of ING2 (Fig.=20 3a; data not shown). Moreover, the H3K4me3 interaction was mostly = abolished=20 by the D230A mutation and several additional substitutions that disrupt=20 H3K4me3-binding in vitro12=20 (Fig.=20 3a, b;=20 data not shown). We conclude that the PHD domain is required for the = association=20 of ING2 with H3K4me3 at chromatin in vivo.

Figure=20 3: The ING2 interaction with trimethylated H3K4 occurs in = vivo=20 and requires an intact PHD domain.

a, b, In vivo association of = wild-type, but not=20 PHD domain mutant, ING2 proteins with H3K4me3 at chromatin. Western = analysis of=20 proteins crosslinked in situ to wild-type or mutant Flag=96ING2 = proteins in=20 protein=96protein ChIPs. Note equal binding of mutant and wild-type ING2 = to SAP30=20 (a) and HDAC1 (b). Input loaded represents 5% of total. = c,=20 Decreased H3K4me3 levels following WDR5 knockdown. Western analysis of = HEK293T=20 cells transfected with WDR5 or control RNA interference (RNAi) = vectors.=20 d, Flag=96ING2 association with endogenous H3 requires H3K4me3. = Western=20 analysis of protein=96protein ChIPs as in a with or without WDR5 = knockdown.=20 e, Endogenous association of H3 and ING2 requires H3K4me3. = Western=20 analysis of H3-bound proteins by protein=96protein ChIP, with or without = WDR5=20 knockdown. f, WDR5 knockdown decreases ING2 occupancy at the = cyclin D1=20 promoter. Levels (per cent input =3D ChIP/input 3Dtimes=20 100) of cyclin D1 promoter and 3' coding = region sequences=20 in the indicated ChIPs, with or without WDR5 knockdown. Error bars = indicate the=20 s.e.m. from three independent experiments.

High=20 resolution image and legend (63K)

To determine whether endogenous H3K4me3 is important for = ING2=20 association with H3, we knocked down the expression of the = methyltransferase=20 component, the WD40-repeat protein WDR5, which leads to a specific = reduction in=20 H3K4me3 levels (Fig.=20 3c)16.=20 This was accompanied by substantially reduced binding of both = Flag-tagged and=20 endogenous ING2 to H3 at chromatin (without affecting complex formation = with=20 HDAC1) (Fig.=20 3d, e).=20 Thus, H3K4me3 is required for interaction of ING2 with H3, and = endogenous ING2=20 specifically associates with trimethylated H3K4 at chromatin in = vivo.

To investigate ING2 association with chromatin at a = target gene,=20 we focused on the cell-cycle regulator cyclin D1. This gene is = transcriptionally=20 inactivated by the mSin3a=96HDAC1 complex17.=20 In ChIP analyses, Flag=96ING2 (and tri- and di-methylated H3K4, as = expected3,=20 4)=20 are specifically detected at the cyclin D1 promoter but not at 3' coding = regions=20 (Fig.=20 3f; Supplementary=20 Fig. S6a). Furthermore, WDR5 knockdown decreased ING2 occupancy at = the=20 cyclin D1 promoter (Fig.=20 3f). Thus, trimethylation of H3K4 is important for ING2 association = at the=20 cyclin D1 promoter.

To investigate the biological significance of the = ING2=96H3K4me3=20 interaction, we used an ING2 complementation system7,=20 whereby RNA interference (RNAi)-resistant wild-type or mutant (D230A or = PHD) ING2 constructs were stably expressed in = ING2=20 knockdown cells. ING2 expression was substantially reduced in the = knockdown=20 cells, and the different ING2 constructs reconstituted expression at = comparable=20 levels (Fig.=20 4a). Notably, the ING2 knockdown cells showed impaired cyclin D1 = mRNA=20 repression in response to doxorubicin compared with control (wild-type) = cells,=20 and complementation of knockdown cells with wild-type ING2 mostly = restored=20 efficient cyclin D1 repression (Fig.=20 4b). In contrast, the ING2D230A and ING23DDelta=20PHD proteins showed significantly = reduced=20 reconstitution activities (Fig.=20 4c). Thus, PHD domain recognition of H3K4me3 is important for = ING2-mediated=20 repression of cyclin D1 mRNA expression in response to DNA damage.

Figure=20 4: Recognition of H3K4me3 by ING2 PHD domain in vivo is = critical=20 for ING2 function.

a, Western analysis of ING2 expression in the = indicated cell=20 lines. *, endogenous ING2. b, ING2 is required for repression of = cyclin=20 D1 expression in response to doxorubicin (dox). Quantitative PCR of = cyclin D1=20 mRNA, with or without doxorubicin (0.2 3Dmicro=20g ml-1, 24 h), in wild-type ("WT"), = knockdown=20 ("KD") and knockdown reconstituted with ING2 ("KD + ING2") cell lines. = c,=20 Impaired activity of mutant ING2 proteins in reconstitution of=20 doxorubicin-dependent cyclin D1 repression, as in b, relative to=20 wild-type ING2 ("KD + ING2"). In b and c, error bars = indicate the=20 s.e.m. of triplicate experiments; P-values < 0.01. = d=96f,=20 DNA-damage-dependent increase of ING2=96HDAC1 occupancy at the cyclin D1 = promoter=20 requires methylated H3K4-binding. ChIPs with antibodies to Flag = (d),=20 HDAC1 (e) and H4K8ac (f) at the cyclin D1 promoter in the=20 indicated cell lines, with or without doxorubicin (2 3Dmicro=20M, 1 h). Error bars indicate the s.e.m. of at least = three=20 independent experiments. P-values < 0.05. g, Western = analysis=20 of cyclin D1 protein in the indicated cell lines with or without = doxorubicin=20 (0.2 3Dmicro=20g ml-1, 24 h). h, Impaired = doxorubicin=20 sensitivity following ING2 knockdown or reconstitution with=20 H3K4me3-binding-defective ING2. Relative cell viability is normalized to = untreated cells. Error bars indicate the s.e.m. of 3=966 independent=20 experiments.

High=20 resolution image and legend (71K)

Next, we examined promoter occupancy of the ING2=96HDAC1 = complexes=20 in response to DNA damage. Doxorubicin treatment increased promoter = occupancy of=20 wild-type, but not mutant, ING2 at the cyclin D1 promoter (Fig.=20 4d), as well as a second HDAC1-regulated DNA-damage response gene,=20 c-Myc (Supplementary=20 Fig. S7)18.=20 Furthermore, HDAC1 occupancy and histone deacetylation at the cyclin D1 = promoter=20 both increased on DNA damage, and these responses, which were largely = abrogated=20 in the knockdown cells, were restored by reconstitution with wild-type, = but not=20 mutant, ING2 (Fig.=20 4e, f).=20 H3K4me2, H3K4me3 and H3 levels were uniform across the different cell = lines and=20 not altered by doxorubicin treatment (Supplementary=20 Fig. S6b). On western analysis, cyclin D1 protein levels were = repressed=20 following DNA damage in the presence of wild-type ING2 (in both control = cells=20 and knockdown cells reconstituted with ING2), but only slightly reduced = in the=20 knockdown cells or knockdown cells reconstituted with mutant ING2 = proteins (Fig.=20 4g). We conclude that recognition of H3K4me3 by the ING2 PHD domain = is=20 critical for proper occupancy of the ING2=96HDAC1 complex at target = promoters=20 during DNA damage responses and active transcriptional repression of the = promoter's cognate gene.

Finally, H3K4me3 recognition by the PHD domain is = critical for=20 ING2 regulation of cellular functions. Specifically, ING2 knockdown=20 significantly impairs cellular sensitivity to doxorubicin (Fig.=20 4h), and reconstitution of knockdown cells with wild-type, but not = mutant,=20 ING2 reverses this effect (Fig.=20 4h). Together, these data argue that the H3K4me3-binding activity of = ING2 is=20 critical for ING2 function in the cellular response to DNA damage.

Our findings and previous work demonstrate that the PHD = domain of=20 ING2 is a dual-specificity module that binds both PtdIns(5)P and = H3K4me3. These=20 activities are separable by specific mutations within the domain, and = both seem=20 critical for ING2 cellular functions. It is possible that = PtdIns(5)P-binding=20 could mediate trafficking of ING2 to target promoters, where binding to = H3K4me3=20 then contributes to retention of ING2 at these promoters (see Supplementary=20 Fig. S8). In this regard, the multi-functionality of the ING2 PHD = domain may=20 contribute to integrating complex nuclear signalling events that link = DNA damage=20 to chromatin responses.

Methylation of H3K4 is proposed to have a pivotal role = in gene=20 activation by serving as a binding platform for different=20 transcription-promoting factors16,=20 19,=20 20,=20 21.=20 Our findings identify the ING2 PHD domain as the first effector domain = for=20 methylated H3K4 that links this modification to transcriptional = repression. By=20 focusing HDAC1 repressor complexes on actively transcribed genes, = recognition of=20 H3K4me3 by ING2 may be important for the efficiency of acute gene = repression.=20 Such a mechanism may be particularly important in the context of = cellular=20 responses to acute stress, such as DNA damage, in which rapid shut-off = of=20 proliferation genes is critical to prevent propagation of cells = harbouring=20 damaged DNA. The PHD domains of the other ING proteins also bind = methylated=20 H3K4, and thus may link this modification to additional cellular = functions.=20 Moreover, the PHD domain of the nucleosome remodelling factor (NURF) = complex=20 component BPTF (bromodomain and PHD domain transcription factor) also = recognizes=20 methylated H3K4 (ref. 22),=20 suggesting a more general role for PHD domains as methyl-lysine effector = domains. Together, our findings highlight the notion that the = recognition of=20 chromatin modifications by effector proteins, rather than the specific=20 modification per se, determines biological function, and, as = such,=20 greatly expands the diversity of signalling at chromatin.

Methods

Histone peptide binding assays

Biotinylated=20 histone peptides were synthesized at Stanford Protein and Nucleic = Acid=20 facility or purchased from Upstate Biotechnology. Briefly, 0.5 3Dmicrog of peptides were incubated with 1 3Dmicro=20g of protein in binding buffer (50 mM Tris-HCl, = pH 7.5,=20 300 mM NaCl, 0.1% (v/v) NP-40, 1 mM phenylmethylsulphonyl = fluoride=20 (PMSF)) overnight at 4 =B0C. After 1 h of incubation, streptavidin=20 beads (Amersham) were washed three times and subjected to western=20 analysis.

Protein=96protein ChIP assays for detection of in = situ=20 ING2=96histone interactions was performed as described15.=20 Cell viability assays were performed as described23.=20 Information about antibodies, recombinant vectors, RNAi sequences and = primers=20 are available in Supplementary=20 Information and on request. Detailed methods can be found in Supplementary=20 Information.

Acknowledgments

We thank Y. Zhang for the SET7 expression vector, C. = Harris for=20 ING3, ING4 and ING5 complementary DNAs, J. Wysocka and W. Herr for a = WDR5=20 antibody, J. Wysocka and C. D. Allis for communicating unpublished = results, J.=20 Yuan for ING2 antibodies and A. Sanchez for peptide synthesis. This work = was=20 supported by NIH grants to O.G., Y.S. and B.R.C. O.G. is a recipient of = a=20 Burroughs Wellcome Career Development Award in Biomedical Sciences.

Competing interests statement:

The authors declared no competing interests.

Supplementary=20 information accompanies this paper.

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  1. Department of Biological Sciences, Stanford University, = and
  2. Department of Medicine, Stanford University School of = Medicine,=20 Stanford, California 94305, USA
  3. Department of Pharmacology, University of Colorado Health = Sciences=20 Center, Aurora, Colorado 80045, USA
  4. Department of Pathology, Harvard Medical School, Boston,=20 Massachusetts 02115, USA
  5. Huntsman Cancer Institute and Department of Oncological = Sciences,=20 University of Utah, Salt Lake City, Utah 84112, USA
  6. Laval University Cancer Research Center, Quebec City, = Quebec G1R=20 2J6, Canada
  7. 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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ISSN: 0028-0836

EISSN: 1476-4687

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