The Dnmt3a PWWP Domain Reads Histone 3 Lysine 36 Trimethylation and Guides DNA Methylation
The Dnmt3a DNA methyltransferase contains in its N-terminal part a PWWP domain that is involved in chromatin targeting. Here, we have investigated the interaction of the PWWP domain with modified histone tails using peptide arrays and show that it specifically recognizes the histone 3 lysine 36 trim...
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| Veröffentlicht in: | The Journal of biological chemistry 2010-08, Vol.285 (34), p.26114-26120 |
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| container_title | The Journal of biological chemistry |
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| creator | Dhayalan, Arunkumar Rajavelu, Arumugam Rathert, Philipp Tamas, Raluca Jurkowska, Renata Z. Ragozin, Sergey Jeltsch, Albert |
| description | The Dnmt3a DNA methyltransferase contains in its N-terminal part a PWWP domain that is involved in chromatin targeting. Here, we have investigated the interaction of the PWWP domain with modified histone tails using peptide arrays and show that it specifically recognizes the histone 3 lysine 36 trimethylation mark. H3K36me3 is known to be a repressive modification correlated with DNA methylation in mammals and heterochromatin in Schizosaccharomyces pombe. These results were confirmed by equilibrium peptide binding studies and pulldown experiments with native histones and purified native nucleosomes. The PWWP-H3K36me3 interaction is important for the subnuclear localization of enhanced yellow fluorescent protein-fused Dnmt3a. Furthermore, the PWWP-H3K36me3 interaction increases the activity of Dnmt3a for methylation of nucleosomal DNA as observed using native nucleosomes isolated from human cells after demethylation of the DNA with 5-aza-2′-deoxycytidine as substrate for methylation with Dnmt3a. These data suggest that the interaction of the PWWP domain with H3K36me3 is involved in targeting of Dnmt3a to chromatin carrying that mark, a model that is in agreement with several studies on the genome-wide distribution of DNA methylation and H3K36me3. |
| doi_str_mv | 10.1074/jbc.M109.089433 |
| format | Article |
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Here, we have investigated the interaction of the PWWP domain with modified histone tails using peptide arrays and show that it specifically recognizes the histone 3 lysine 36 trimethylation mark. H3K36me3 is known to be a repressive modification correlated with DNA methylation in mammals and heterochromatin in Schizosaccharomyces pombe. These results were confirmed by equilibrium peptide binding studies and pulldown experiments with native histones and purified native nucleosomes. The PWWP-H3K36me3 interaction is important for the subnuclear localization of enhanced yellow fluorescent protein-fused Dnmt3a. Furthermore, the PWWP-H3K36me3 interaction increases the activity of Dnmt3a for methylation of nucleosomal DNA as observed using native nucleosomes isolated from human cells after demethylation of the DNA with 5-aza-2′-deoxycytidine as substrate for methylation with Dnmt3a. These data suggest that the interaction of the PWWP domain with H3K36me3 is involved in targeting of Dnmt3a to chromatin carrying that mark, a model that is in agreement with several studies on the genome-wide distribution of DNA methylation and H3K36me3.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M109.089433</identifier><identifier>PMID: 20547484</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Cell Line ; Chromatin Histone Modification ; DNA (Cytosine-5-)-Methyltransferases - genetics ; DNA (Cytosine-5-)-Methyltransferases - physiology ; DNA and Chromosomes ; DNA Methylation ; DNA Methyltransferase ; Epigenetics ; Histone Methylation ; Histones - metabolism ; Humans ; Lysine - metabolism ; Methylation ; Mice ; Protein Array Analysis ; Protein Binding ; Protein Structure, Tertiary ; Schizosaccharomyces pombe ; Transfection</subject><ispartof>The Journal of biological chemistry, 2010-08, Vol.285 (34), p.26114-26120</ispartof><rights>2010 © 2010 ASBMB. 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Here, we have investigated the interaction of the PWWP domain with modified histone tails using peptide arrays and show that it specifically recognizes the histone 3 lysine 36 trimethylation mark. H3K36me3 is known to be a repressive modification correlated with DNA methylation in mammals and heterochromatin in Schizosaccharomyces pombe. These results were confirmed by equilibrium peptide binding studies and pulldown experiments with native histones and purified native nucleosomes. The PWWP-H3K36me3 interaction is important for the subnuclear localization of enhanced yellow fluorescent protein-fused Dnmt3a. Furthermore, the PWWP-H3K36me3 interaction increases the activity of Dnmt3a for methylation of nucleosomal DNA as observed using native nucleosomes isolated from human cells after demethylation of the DNA with 5-aza-2′-deoxycytidine as substrate for methylation with Dnmt3a. These data suggest that the interaction of the PWWP domain with H3K36me3 is involved in targeting of Dnmt3a to chromatin carrying that mark, a model that is in agreement with several studies on the genome-wide distribution of DNA methylation and H3K36me3.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Chromatin Histone Modification</subject><subject>DNA (Cytosine-5-)-Methyltransferases - genetics</subject><subject>DNA (Cytosine-5-)-Methyltransferases - physiology</subject><subject>DNA and Chromosomes</subject><subject>DNA Methylation</subject><subject>DNA Methyltransferase</subject><subject>Epigenetics</subject><subject>Histone Methylation</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Lysine - metabolism</subject><subject>Methylation</subject><subject>Mice</subject><subject>Protein Array Analysis</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Schizosaccharomyces pombe</subject><subject>Transfection</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcFvFCEUxonR2LX17E25eZotMDDAxaTpamuytU27TY0X8gaYLs3M0A6zTfa_l83UqgcjF0je733vfXwIvaNkTonkh3e1nZ9RoudEaV6WL9CMElUWpaDfX6IZIYwWmgm1h96kdEfy4Zq-RnuMCC654jP0Y7X2eNF3Ywn44ubmAi9iB6HHlx5cwqchjbH3uMTLbQq7R4VXQ-j8uN62MIbYY-gdPtkE5xNefDvCZ79LB-hVA23yb5_ufXT95fPq-LRYnp98PT5aFraiZCx0DQ5cU1MHlcguKuqsa4ALAF4xKxtlNahKA9SVFI1tdm2ltt5qxWw2vY8-Tbr3m7rzzvp-HKA193lPGLYmQjB_V_qwNrfx0TDNOKE8C3x8Ehjiw8an0XQhWd-20Pu4SUZWjElNqPg_yZUWTHOVycOJtENMafDN8z6UmF10JkdndtGZKbrc8f5PG8_8r6wy8GECGogGboeQzPUVI7QkVEkpqMyEngifv_sx-MEkG3xvvQuDt6NxMfxz_E-I7rG2</recordid><startdate>20100820</startdate><enddate>20100820</enddate><creator>Dhayalan, Arunkumar</creator><creator>Rajavelu, Arumugam</creator><creator>Rathert, Philipp</creator><creator>Tamas, Raluca</creator><creator>Jurkowska, Renata Z.</creator><creator>Ragozin, Sergey</creator><creator>Jeltsch, Albert</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>FBQ</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7TM</scope><scope>5PM</scope></search><sort><creationdate>20100820</creationdate><title>The Dnmt3a PWWP Domain Reads Histone 3 Lysine 36 Trimethylation and Guides DNA Methylation</title><author>Dhayalan, Arunkumar ; 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Here, we have investigated the interaction of the PWWP domain with modified histone tails using peptide arrays and show that it specifically recognizes the histone 3 lysine 36 trimethylation mark. H3K36me3 is known to be a repressive modification correlated with DNA methylation in mammals and heterochromatin in Schizosaccharomyces pombe. These results were confirmed by equilibrium peptide binding studies and pulldown experiments with native histones and purified native nucleosomes. The PWWP-H3K36me3 interaction is important for the subnuclear localization of enhanced yellow fluorescent protein-fused Dnmt3a. Furthermore, the PWWP-H3K36me3 interaction increases the activity of Dnmt3a for methylation of nucleosomal DNA as observed using native nucleosomes isolated from human cells after demethylation of the DNA with 5-aza-2′-deoxycytidine as substrate for methylation with Dnmt3a. 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| subjects | Animals Cell Line Chromatin Histone Modification DNA (Cytosine-5-)-Methyltransferases - genetics DNA (Cytosine-5-)-Methyltransferases - physiology DNA and Chromosomes DNA Methylation DNA Methyltransferase Epigenetics Histone Methylation Histones - metabolism Humans Lysine - metabolism Methylation Mice Protein Array Analysis Protein Binding Protein Structure, Tertiary Schizosaccharomyces pombe Transfection |
| title | The Dnmt3a PWWP Domain Reads Histone 3 Lysine 36 Trimethylation and Guides DNA Methylation |
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