Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells
Acetylation and other modifications on histones comprise histone codes that govern transcriptional regulatory processes in chromatin. Yet little is known how different histone codes are translated and put into action. Using fluorescence resonance energy transfer, we show that bromodomain-containing...
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| Veröffentlicht in: | Molecular cell 2004-01, Vol.13 (1), p.33-43 |
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| creator | Kanno, Tomohiko Kanno, Yuka Siegel, Richard M Jang, Moon Kyoo Lenardo, Michael J Ozato, Keiko |
| description | Acetylation and other modifications on histones comprise histone codes that govern transcriptional regulatory processes in chromatin. Yet little is known how different histone codes are translated and put into action. Using fluorescence resonance energy transfer, we show that bromodomain-containing proteins recognize different patterns of acetylated histones in intact nuclei of living cells. The bromodomain protein Brd2 selectively interacted with acetylated lysine 12 on histone H4, whereas TAF
II250 and PCAF recognized H3 and other acetylated histones, indicating fine specificity of histone recognition by different bromodomains. This hierarchy of interactions was also seen in direct peptide binding assays. Interaction with acetylated histone was essential for Brd2 to amplify transcription. Moreover association of Brd2, but not other bromodomain proteins, with acetylated chromatin persisted on chromosomes during mitosis. Thus the recognition of histone acetylation code by bromodomains is selective, is involved in transcription, and potentially conveys transcriptional memory across cell divisions. |
| doi_str_mv | 10.1016/S1097-2765(03)00482-9 |
| format | Article |
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II250 and PCAF recognized H3 and other acetylated histones, indicating fine specificity of histone recognition by different bromodomains. This hierarchy of interactions was also seen in direct peptide binding assays. Interaction with acetylated histone was essential for Brd2 to amplify transcription. Moreover association of Brd2, but not other bromodomain proteins, with acetylated chromatin persisted on chromosomes during mitosis. Thus the recognition of histone acetylation code by bromodomains is selective, is involved in transcription, and potentially conveys transcriptional memory across cell divisions.</description><identifier>ISSN: 1097-2765</identifier><identifier>EISSN: 1097-4164</identifier><identifier>DOI: 10.1016/S1097-2765(03)00482-9</identifier><identifier>PMID: 14731392</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Acetylation ; Animals ; Base Sequence ; Brd2 protein ; Cell Nucleus - metabolism ; HeLa Cells ; Histones - chemistry ; Histones - metabolism ; Humans ; Mice ; Mitosis ; NIH 3T3 Cells ; PCAF protein ; Point Mutation ; Protein Binding ; Protein Structure, Tertiary ; Recombinant Fusion Proteins - metabolism ; TAFII250 protein ; Transcription, Genetic</subject><ispartof>Molecular cell, 2004-01, Vol.13 (1), p.33-43</ispartof><rights>2004 Cell Press</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c505t-9a33189451beb7b5a244ecfa024234b780393cd1ffe591705f4c28a11ea04eda3</citedby><cites>FETCH-LOGICAL-c505t-9a33189451beb7b5a244ecfa024234b780393cd1ffe591705f4c28a11ea04eda3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/S1097-2765(03)00482-9$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/14731392$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kanno, Tomohiko</creatorcontrib><creatorcontrib>Kanno, Yuka</creatorcontrib><creatorcontrib>Siegel, Richard M</creatorcontrib><creatorcontrib>Jang, Moon Kyoo</creatorcontrib><creatorcontrib>Lenardo, Michael J</creatorcontrib><creatorcontrib>Ozato, Keiko</creatorcontrib><title>Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells</title><title>Molecular cell</title><addtitle>Mol Cell</addtitle><description>Acetylation and other modifications on histones comprise histone codes that govern transcriptional regulatory processes in chromatin. Yet little is known how different histone codes are translated and put into action. Using fluorescence resonance energy transfer, we show that bromodomain-containing proteins recognize different patterns of acetylated histones in intact nuclei of living cells. The bromodomain protein Brd2 selectively interacted with acetylated lysine 12 on histone H4, whereas TAF
II250 and PCAF recognized H3 and other acetylated histones, indicating fine specificity of histone recognition by different bromodomains. This hierarchy of interactions was also seen in direct peptide binding assays. Interaction with acetylated histone was essential for Brd2 to amplify transcription. Moreover association of Brd2, but not other bromodomain proteins, with acetylated chromatin persisted on chromosomes during mitosis. Thus the recognition of histone acetylation code by bromodomains is selective, is involved in transcription, and potentially conveys transcriptional memory across cell divisions.</description><subject>Acetylation</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Brd2 protein</subject><subject>Cell Nucleus - metabolism</subject><subject>HeLa Cells</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Mice</subject><subject>Mitosis</subject><subject>NIH 3T3 Cells</subject><subject>PCAF protein</subject><subject>Point Mutation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>TAFII250 protein</subject><subject>Transcription, Genetic</subject><issn>1097-2765</issn><issn>1097-4164</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU1r3DAQhkVo6Kab_oQUnUp7cDJjSWvrVDZLkxQWEpqPq5DlcVCxra3kXdj8-no_oMecZhiemXd4X8YuEC4RcHb1iKCLLC9m6huI7wCyzDN9ws72Y4kz-eHY75AJ-5TSHwCUqtQf2QRlIVDo_IyZR2rJDX5D_De58Nr7wYeeh4bPHQ3b1g5U8zufhtBT4tWWX8fQhTp01vf8IYaBfJ_4i09r2_q3kR3HS7_x_StfUNumc3ba2DbR52Odsuebn0-Lu2x5f_trMV9mToEaMm2FwFJLhRVVRaVsLiW5xkIucyGrogShhauxaUhpLEA10uWlRSQLkmorpuzr4e4qhr9rSoPpfHLjB7ansE6mBIRZifpdEHWuQJRqBNUBdDGkFKkxq-g7G7cGwewiMPsIzM5fA8LsIzA7gS9HgXXVUf1_6-j5CPw4ADT6sfEUTXKeeke1j2MUpg7-HYl_yfSWYQ</recordid><startdate>20040116</startdate><enddate>20040116</enddate><creator>Kanno, Tomohiko</creator><creator>Kanno, Yuka</creator><creator>Siegel, Richard M</creator><creator>Jang, Moon Kyoo</creator><creator>Lenardo, Michael J</creator><creator>Ozato, Keiko</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20040116</creationdate><title>Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells</title><author>Kanno, Tomohiko ; Kanno, Yuka ; Siegel, Richard M ; Jang, Moon Kyoo ; Lenardo, Michael J ; Ozato, Keiko</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c505t-9a33189451beb7b5a244ecfa024234b780393cd1ffe591705f4c28a11ea04eda3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Acetylation</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Brd2 protein</topic><topic>Cell Nucleus - metabolism</topic><topic>HeLa Cells</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Mice</topic><topic>Mitosis</topic><topic>NIH 3T3 Cells</topic><topic>PCAF protein</topic><topic>Point Mutation</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>TAFII250 protein</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kanno, Tomohiko</creatorcontrib><creatorcontrib>Kanno, Yuka</creatorcontrib><creatorcontrib>Siegel, Richard M</creatorcontrib><creatorcontrib>Jang, Moon Kyoo</creatorcontrib><creatorcontrib>Lenardo, Michael J</creatorcontrib><creatorcontrib>Ozato, Keiko</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>MEDLINE - Academic</collection><jtitle>Molecular cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kanno, Tomohiko</au><au>Kanno, Yuka</au><au>Siegel, Richard M</au><au>Jang, Moon Kyoo</au><au>Lenardo, Michael J</au><au>Ozato, Keiko</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells</atitle><jtitle>Molecular cell</jtitle><addtitle>Mol Cell</addtitle><date>2004-01-16</date><risdate>2004</risdate><volume>13</volume><issue>1</issue><spage>33</spage><epage>43</epage><pages>33-43</pages><issn>1097-2765</issn><eissn>1097-4164</eissn><abstract>Acetylation and other modifications on histones comprise histone codes that govern transcriptional regulatory processes in chromatin. 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II250 and PCAF recognized H3 and other acetylated histones, indicating fine specificity of histone recognition by different bromodomains. This hierarchy of interactions was also seen in direct peptide binding assays. Interaction with acetylated histone was essential for Brd2 to amplify transcription. Moreover association of Brd2, but not other bromodomain proteins, with acetylated chromatin persisted on chromosomes during mitosis. Thus the recognition of histone acetylation code by bromodomains is selective, is involved in transcription, and potentially conveys transcriptional memory across cell divisions.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>14731392</pmid><doi>10.1016/S1097-2765(03)00482-9</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylation Animals Base Sequence Brd2 protein Cell Nucleus - metabolism HeLa Cells Histones - chemistry Histones - metabolism Humans Mice Mitosis NIH 3T3 Cells PCAF protein Point Mutation Protein Binding Protein Structure, Tertiary Recombinant Fusion Proteins - metabolism TAFII250 protein Transcription, Genetic |
| title | Selective Recognition of Acetylated Histones by Bromodomain Proteins Visualized in Living Cells |
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