A Trithorax-Group Complex Purified from Saccharomyces cerevisiae is Required for Methylation of Histone H3
Histone methylation has emerged as an important mechanism for regulating the transcriptional accessibility of chromatin. Several methyltransferases have been shown to target histone aminoterminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the bi...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2002-01, Vol.99 (1), p.90-94 |
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| creator | Nagy, Peter L. Griesenbeck, Joachim Kornberg, Roger D. Cleary, Michael L. |
| description | Histone methylation has emerged as an important mechanism for regulating the transcriptional accessibility of chromatin. Several methyltransferases have been shown to target histone aminoterminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events has not been well characterized. We report here the purification, molecular identification, and genetic and biochemical characterization of the Set1 protein complex that is necessary for methylation of histone H3 at lysine residue 4 in Saccharomyces cerevisiae. The seven-member 363-kDa complex contains homologs of Drosophila melanogaster proteins Ash2 and Trithorax and Caenorhabditis elegans protein DPY-30, which are implicated in the maintenance of Hox gene expression and regulation of X chromosome dosage compensation, respectively. Mutations of Set1 protein comparable to those that disrupt developmental function of its Drosophila homolog Trithorax abrogate histone methylation in yeast. These studies suggest that epigenetic regulation of developmental and sex-specific gene expression are species-specific readouts for a common chromatin remodeling machinery associated mechanistically with histone methylation. |
| doi_str_mv | 10.1073/pnas.221596698 |
| format | Article |
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Several methyltransferases have been shown to target histone aminoterminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events has not been well characterized. We report here the purification, molecular identification, and genetic and biochemical characterization of the Set1 protein complex that is necessary for methylation of histone H3 at lysine residue 4 in Saccharomyces cerevisiae. The seven-member 363-kDa complex contains homologs of Drosophila melanogaster proteins Ash2 and Trithorax and Caenorhabditis elegans protein DPY-30, which are implicated in the maintenance of Hox gene expression and regulation of X chromosome dosage compensation, respectively. Mutations of Set1 protein comparable to those that disrupt developmental function of its Drosophila homolog Trithorax abrogate histone methylation in yeast. 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Several methyltransferases have been shown to target histone aminoterminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events has not been well characterized. We report here the purification, molecular identification, and genetic and biochemical characterization of the Set1 protein complex that is necessary for methylation of histone H3 at lysine residue 4 in Saccharomyces cerevisiae. The seven-member 363-kDa complex contains homologs of Drosophila melanogaster proteins Ash2 and Trithorax and Caenorhabditis elegans protein DPY-30, which are implicated in the maintenance of Hox gene expression and regulation of X chromosome dosage compensation, respectively. Mutations of Set1 protein comparable to those that disrupt developmental function of its Drosophila homolog Trithorax abrogate histone methylation in yeast. These studies suggest that epigenetic regulation of developmental and sex-specific gene expression are species-specific readouts for a common chromatin remodeling machinery associated mechanistically with histone methylation.</description><subject>Animals</subject><subject>Ash2 protein</subject><subject>Biological Sciences</subject><subject>Biology</subject><subject>Caenorhabditis elegans - chemistry</subject><subject>Caenorhabditis elegans Proteins</subject><subject>Chromatin</subject><subject>Chromatin - chemistry</subject><subject>Chromatin - metabolism</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Dosage Compensation, Genetic</subject><subject>DPY-30 protein</subject><subject>Drosophila</subject><subject>Drosophila melanogaster</subject><subject>Drosophila Proteins</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Gels</subject><subject>Gene expression</subject><subject>Gene expression regulation</subject><subject>Genes</subject><subject>Genetics</subject><subject>histone H3</subject><subject>Histone-Lysine N-Methyltransferase</subject><subject>Histones</subject><subject>Histones - metabolism</subject><subject>Lysine - chemistry</subject><subject>Methylation</subject><subject>Models, Genetic</subject><subject>Mutation</subject><subject>Nuclear Proteins - chemistry</subject><subject>Phenotype</subject><subject>Phenotypes</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Set1 protein</subject><subject>Sex Factors</subject><subject>Studies</subject><subject>Transcription Factors - metabolism</subject><subject>Trithorax protein</subject><subject>X Chromosome</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc-L1DAYhoMo7rh69aJIkMVbx3xp0jQHD8vg7ggriq7nkMl8dTK0TTdpl5n_3pYZxx8gnhJ4nzfk-x5CngObA1P52661ac45SF0UunxAZsA0ZIXQ7CGZMcZVVgouzsiTlLaMMS1L9picASjJBfAZ2V7S2-j7TYh2l13HMHR0EZquxh39PERfeVzTKoaGfrXObex42ztM1GHEe5-8ReoT_YJ3g48TGSL9iP1mX9veh5aGii596kOLdJk_JY8qWyd8djzPyber97eLZXbz6frD4vImcxLyPiuVK4TUWoBjlXRrLVnJK4WFFIDK5qBRr5jUKHMAnuPKKilQOpRgrSvW-Tl5d3i3G1YNrh22fbS16aJvbNybYL35M2n9xnwP92baCuix_-bYj-FuwNSbxieHdW1bDEMyCnJZFlr9F4SSc8aFGMHXf4HbMMR2XILhDIQACRM0P0AuhpQiVqcfAzOTazO5NifXY-HV73P-wo9yR-DiCEzFn7HWBoxmphrqusddP2Iv_o2N6ctDuh09xlOcM6mELvIfA3nF9w</recordid><startdate>20020108</startdate><enddate>20020108</enddate><creator>Nagy, Peter L.</creator><creator>Griesenbeck, Joachim</creator><creator>Kornberg, Roger D.</creator><creator>Cleary, Michael L.</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><general>The National Academy of Sciences</general><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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20020108</creationdate><title>A Trithorax-Group Complex Purified from Saccharomyces cerevisiae is Required for Methylation of Histone H3</title><author>Nagy, Peter L. ; Griesenbeck, Joachim ; Kornberg, Roger D. ; Cleary, Michael L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c513t-87c6459941c0f5cd95082f7e6541e7a319e9b059e531123eba754e5ce51aac6d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Animals</topic><topic>Ash2 protein</topic><topic>Biological Sciences</topic><topic>Biology</topic><topic>Caenorhabditis elegans - chemistry</topic><topic>Caenorhabditis elegans Proteins</topic><topic>Chromatin</topic><topic>Chromatin - chemistry</topic><topic>Chromatin - metabolism</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Dosage Compensation, Genetic</topic><topic>DPY-30 protein</topic><topic>Drosophila</topic><topic>Drosophila melanogaster</topic><topic>Drosophila Proteins</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Gels</topic><topic>Gene expression</topic><topic>Gene expression regulation</topic><topic>Genes</topic><topic>Genetics</topic><topic>histone H3</topic><topic>Histone-Lysine N-Methyltransferase</topic><topic>Histones</topic><topic>Histones - metabolism</topic><topic>Lysine - chemistry</topic><topic>Methylation</topic><topic>Models, Genetic</topic><topic>Mutation</topic><topic>Nuclear Proteins - chemistry</topic><topic>Phenotype</topic><topic>Phenotypes</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Proteins</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Set1 protein</topic><topic>Sex Factors</topic><topic>Studies</topic><topic>Transcription Factors - metabolism</topic><topic>Trithorax protein</topic><topic>X Chromosome</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nagy, Peter L.</creatorcontrib><creatorcontrib>Griesenbeck, Joachim</creatorcontrib><creatorcontrib>Kornberg, Roger D.</creatorcontrib><creatorcontrib>Cleary, Michael L.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nagy, Peter L.</au><au>Griesenbeck, Joachim</au><au>Kornberg, Roger D.</au><au>Cleary, Michael L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A Trithorax-Group Complex Purified from Saccharomyces cerevisiae is Required for Methylation of Histone H3</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2002-01-08</date><risdate>2002</risdate><volume>99</volume><issue>1</issue><spage>90</spage><epage>94</epage><pages>90-94</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Histone methylation has emerged as an important mechanism for regulating the transcriptional accessibility of chromatin. Several methyltransferases have been shown to target histone aminoterminal tails and mark nucleosomes associated with either euchromatic or heterochromatic states. However, the biochemical machinery responsible for regulating histone methylation and integrating it with other cellular events has not been well characterized. We report here the purification, molecular identification, and genetic and biochemical characterization of the Set1 protein complex that is necessary for methylation of histone H3 at lysine residue 4 in Saccharomyces cerevisiae. The seven-member 363-kDa complex contains homologs of Drosophila melanogaster proteins Ash2 and Trithorax and Caenorhabditis elegans protein DPY-30, which are implicated in the maintenance of Hox gene expression and regulation of X chromosome dosage compensation, respectively. Mutations of Set1 protein comparable to those that disrupt developmental function of its Drosophila homolog Trithorax abrogate histone methylation in yeast. These studies suggest that epigenetic regulation of developmental and sex-specific gene expression are species-specific readouts for a common chromatin remodeling machinery associated mechanistically with histone methylation.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>11752412</pmid><doi>10.1073/pnas.221596698</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Animals Ash2 protein Biological Sciences Biology Caenorhabditis elegans - chemistry Caenorhabditis elegans Proteins Chromatin Chromatin - chemistry Chromatin - metabolism DNA-Binding Proteins - chemistry DNA-Binding Proteins - metabolism Dosage Compensation, Genetic DPY-30 protein Drosophila Drosophila melanogaster Drosophila Proteins Electrophoresis, Polyacrylamide Gel Gels Gene expression Gene expression regulation Genes Genetics histone H3 Histone-Lysine N-Methyltransferase Histones Histones - metabolism Lysine - chemistry Methylation Models, Genetic Mutation Nuclear Proteins - chemistry Phenotype Phenotypes Protein Binding Protein Structure, Tertiary Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins Set1 protein Sex Factors Studies Transcription Factors - metabolism Trithorax protein X Chromosome Yeasts |
| title | A Trithorax-Group Complex Purified from Saccharomyces cerevisiae is Required for Methylation of Histone H3 |
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