The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex
Transcription is regulated through chromatin remodeling and histone modification, mediated by large protein complexes. Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function...
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| Veröffentlicht in: | The Journal of biological chemistry 2002-03, Vol.277 (10), p.8178-8186 |
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| container_issue | 10 |
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| container_title | The Journal of biological chemistry |
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| creator | Sterner, David E. Wang, Xun Bloom, Melissa H. Simon, Gabriel M. Berger, Shelley L. |
| description | Transcription is regulated through chromatin remodeling and histone modification, mediated by large protein complexes. Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function of two additional domains within the yeast SAGA complex, containing the histone acetyltransferase Gcn5. We have analyzed deletion and substitution mutations within Gcn5 and Ada2, an interacting protein within SAGA, and have identified substrate recognition functions within the SANT domain of Ada2 and regions of the histone acetyltransferase domain of Gcn5 that are distinct from catalytic function itself. These results suggest that histone and nucleosomal substrate recognition by SAGA involves multiple conserved domains and proteins, beyond those that have been previously identified. |
| doi_str_mv | 10.1074/jbc.M108601200 |
| format | Article |
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Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function of two additional domains within the yeast SAGA complex, containing the histone acetyltransferase Gcn5. We have analyzed deletion and substitution mutations within Gcn5 and Ada2, an interacting protein within SAGA, and have identified substrate recognition functions within the SANT domain of Ada2 and regions of the histone acetyltransferase domain of Gcn5 that are distinct from catalytic function itself. 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Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function of two additional domains within the yeast SAGA complex, containing the histone acetyltransferase Gcn5. We have analyzed deletion and substitution mutations within Gcn5 and Ada2, an interacting protein within SAGA, and have identified substrate recognition functions within the SANT domain of Ada2 and regions of the histone acetyltransferase domain of Gcn5 that are distinct from catalytic function itself. These results suggest that histone and nucleosomal substrate recognition by SAGA involves multiple conserved domains and proteins, beyond those that have been previously identified.</description><subject>Acetyltransferases - chemistry</subject><subject>Acetyltransferases - genetics</subject><subject>Acetyltransferases - metabolism</subject><subject>Ada2 protein</subject><subject>Alanine - chemistry</subject><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Binding Sites</subject><subject>Blotting, Western</subject><subject>Chromatin - metabolism</subject><subject>DNA-Binding Proteins</subject><subject>Fungal Proteins - chemistry</subject><subject>Fungal Proteins - metabolism</subject><subject>Gcn5 protein</subject><subject>Gene Deletion</subject><subject>Histone Acetyltransferases</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Mutation</subject><subject>Nucleosomes - metabolism</subject><subject>Phenotype</subject><subject>Plasmids - metabolism</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>Protein Kinases - chemistry</subject><subject>Protein Kinases - metabolism</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structure-Activity Relationship</subject><subject>Substrate Specificity</subject><subject>Temperature</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEFv2yAYQNHUak2zXXeskCrt5hRwbPDRyrYkUptKXSp1J4bhoyGyQwpO2_z70SVST-UCiPc9oYfQN0pGlPDx1brRoxtKREkoI-QTGqRznuUFfThBA0IYzSpWiDN0HuOapDWu6Gd0RinnvKJkgP4uV4B_14sl_uE75TbYW1wbxfA84jt42rkABlsf8MKHTrW41tDvW9U7_x-dudj7DUTc7HGfTH9AxT75pjWe-G7bwusXdGpVG-HrcR-i-18_l5NZdn07nU_q60yP86rPdAV5oZVgrODCWjI2mlkuhAJdCtYQpnh6LW1REV1WurGmMemSNyUoUQmTD9H3g3cb_NMOYi87FzW0rdqA30VJBStFmdMEjg6gDj7GAFZug-tU2EtK5FtTmZrK96Zp4OJo3jUdmHf8GDEBlwdg5R5XL6mYbJzXK-gk4_zNKigXiRIHClKFZwdBRu1go8GkCd1L491HP_gHiziPiw</recordid><startdate>20020308</startdate><enddate>20020308</enddate><creator>Sterner, David E.</creator><creator>Wang, Xun</creator><creator>Bloom, Melissa H.</creator><creator>Simon, Gabriel M.</creator><creator>Berger, Shelley L.</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>M7N</scope></search><sort><creationdate>20020308</creationdate><title>The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex</title><author>Sterner, David E. ; Wang, Xun ; Bloom, Melissa H. ; Simon, Gabriel M. ; Berger, Shelley L.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c439t-c9e35ca822578ff04dc2f788aec682b02a7ca86f590c69cbfdbdf593b6ea898d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Acetyltransferases - chemistry</topic><topic>Acetyltransferases - genetics</topic><topic>Acetyltransferases - metabolism</topic><topic>Ada2 protein</topic><topic>Alanine - chemistry</topic><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Binding Sites</topic><topic>Blotting, Western</topic><topic>Chromatin - metabolism</topic><topic>DNA-Binding Proteins</topic><topic>Fungal Proteins - chemistry</topic><topic>Fungal Proteins - metabolism</topic><topic>Gcn5 protein</topic><topic>Gene Deletion</topic><topic>Histone Acetyltransferases</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Mutation</topic><topic>Nucleosomes - metabolism</topic><topic>Phenotype</topic><topic>Plasmids - metabolism</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>Protein Kinases - chemistry</topic><topic>Protein Kinases - metabolism</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structure-Activity Relationship</topic><topic>Substrate Specificity</topic><topic>Temperature</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Sterner, David E.</creatorcontrib><creatorcontrib>Wang, Xun</creatorcontrib><creatorcontrib>Bloom, Melissa H.</creatorcontrib><creatorcontrib>Simon, Gabriel M.</creatorcontrib><creatorcontrib>Berger, Shelley L.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Sterner, David E.</au><au>Wang, Xun</au><au>Bloom, Melissa H.</au><au>Simon, Gabriel M.</au><au>Berger, Shelley L.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2002-03-08</date><risdate>2002</risdate><volume>277</volume><issue>10</issue><spage>8178</spage><epage>8186</epage><pages>8178-8186</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Transcription is regulated through chromatin remodeling and histone modification, mediated by large protein complexes. Histone and nucleosome interaction has been shown to be mediated by specific chromatin domains called bromodomains and chromodomains. Here we provide evidence for a similar function of two additional domains within the yeast SAGA complex, containing the histone acetyltransferase Gcn5. We have analyzed deletion and substitution mutations within Gcn5 and Ada2, an interacting protein within SAGA, and have identified substrate recognition functions within the SANT domain of Ada2 and regions of the histone acetyltransferase domain of Gcn5 that are distinct from catalytic function itself. These results suggest that histone and nucleosomal substrate recognition by SAGA involves multiple conserved domains and proteins, beyond those that have been previously identified.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11777910</pmid><doi>10.1074/jbc.M108601200</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acetyltransferases - chemistry Acetyltransferases - genetics Acetyltransferases - metabolism Ada2 protein Alanine - chemistry Amino Acid Sequence Animals Binding Sites Blotting, Western Chromatin - metabolism DNA-Binding Proteins Fungal Proteins - chemistry Fungal Proteins - metabolism Gcn5 protein Gene Deletion Histone Acetyltransferases Histones - metabolism Humans Molecular Sequence Data Mutation Nucleosomes - metabolism Phenotype Plasmids - metabolism Precipitin Tests Protein Binding Protein Kinases - chemistry Protein Kinases - metabolism Protein Structure, Tertiary Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Structure-Activity Relationship Substrate Specificity Temperature Transcription Factors - chemistry Transcription Factors - metabolism |
| title | The SANT Domain of Ada2 Is Required for Normal Acetylation of Histones by the Yeast SAGA Complex |
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