Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain
Abstract Yaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the se...
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| Veröffentlicht in: | Nucleic acids research 2018-01, Vol.46 (1), p.421-430 |
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| creator | Klein, Brianna J Ahmad, Salar Vann, Kendra R Andrews, Forest H Mayo, Zachary A Bourriquen, Gaelle Bridgers, Joseph B Zhang, Jinyong Strahl, Brian D Côté, Jacques Kutateladze, Tatiana G |
| description | Abstract
Yaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the sequence C-terminal to K27ac stabilizes the complex. The side chain of K27ac inserts between two aromatic residues, mutation of which abrogates the interaction in vitro and leads in vivo to phenotypes similar to YAF9 deletion, including loss of SWR1-dependent incorporation of variant histone H2A.Z. Our findings reveal the molecular basis for the recognition of H3K27ac by a YEATS reader and underscore the importance of this interaction in mediating Yaf9 function within the NuA4 and SWR1 complexes. |
| doi_str_mv | 10.1093/nar/gkx1151 |
| format | Article |
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Yaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the sequence C-terminal to K27ac stabilizes the complex. The side chain of K27ac inserts between two aromatic residues, mutation of which abrogates the interaction in vitro and leads in vivo to phenotypes similar to YAF9 deletion, including loss of SWR1-dependent incorporation of variant histone H2A.Z. Our findings reveal the molecular basis for the recognition of H3K27ac by a YEATS reader and underscore the importance of this interaction in mediating Yaf9 function within the NuA4 and SWR1 complexes.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkx1151</identifier><identifier>PMID: 29145630</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Acetylation ; Adenosine Triphosphatases - chemistry ; Adenosine Triphosphatases - genetics ; Adenosine Triphosphatases - metabolism ; Amino Acid Sequence ; Binding Sites - genetics ; Histone Acetyltransferases - chemistry ; Histone Acetyltransferases - genetics ; Histone Acetyltransferases - metabolism ; Histones - chemistry ; Histones - metabolism ; Multiprotein Complexes - chemistry ; Multiprotein Complexes - genetics ; Multiprotein Complexes - metabolism ; Protein Domains ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Homology, Amino Acid ; Structural Biology</subject><ispartof>Nucleic acids research, 2018-01, Vol.46 (1), p.421-430</ispartof><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research. 2018</rights><rights>The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c412t-8c1a1ebbff2b3f99014e6dba46833961531e9c42c62a1ece1487d6e2b3c89b0f3</citedby><cites>FETCH-LOGICAL-c412t-8c1a1ebbff2b3f99014e6dba46833961531e9c42c62a1ece1487d6e2b3c89b0f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5758897/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5758897/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,1598,27901,27902,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29145630$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Klein, Brianna J</creatorcontrib><creatorcontrib>Ahmad, Salar</creatorcontrib><creatorcontrib>Vann, Kendra R</creatorcontrib><creatorcontrib>Andrews, Forest H</creatorcontrib><creatorcontrib>Mayo, Zachary A</creatorcontrib><creatorcontrib>Bourriquen, Gaelle</creatorcontrib><creatorcontrib>Bridgers, Joseph B</creatorcontrib><creatorcontrib>Zhang, Jinyong</creatorcontrib><creatorcontrib>Strahl, Brian D</creatorcontrib><creatorcontrib>Côté, Jacques</creatorcontrib><creatorcontrib>Kutateladze, Tatiana G</creatorcontrib><title>Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Abstract
Yaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the sequence C-terminal to K27ac stabilizes the complex. The side chain of K27ac inserts between two aromatic residues, mutation of which abrogates the interaction in vitro and leads in vivo to phenotypes similar to YAF9 deletion, including loss of SWR1-dependent incorporation of variant histone H2A.Z. Our findings reveal the molecular basis for the recognition of H3K27ac by a YEATS reader and underscore the importance of this interaction in mediating Yaf9 function within the NuA4 and SWR1 complexes.</description><subject>Acetylation</subject><subject>Adenosine Triphosphatases - chemistry</subject><subject>Adenosine Triphosphatases - genetics</subject><subject>Adenosine Triphosphatases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Binding Sites - genetics</subject><subject>Histone Acetyltransferases - chemistry</subject><subject>Histone Acetyltransferases - genetics</subject><subject>Histone Acetyltransferases - metabolism</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - genetics</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Protein Domains</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Structural Biology</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>TOX</sourceid><sourceid>EIF</sourceid><recordid>eNp9kV1LHDEUhoNUdP246n3JVRFkNCfJZCc3hUW0itKCH4hQCJnMmd2pM5M1mSn23zeyq-hNr87F-5znHHgJ-QzsCJgWx70Nx_PHZ4AcNsgEhOKZ1Ip_IhMmWJ4Bk8U22YnxN2MgIZdbZJtrkLkSbEJ-Pdha0ziWY98M1Nd0WCD9Mc4ktX1Fb-6vgTrfLVt8xkgHG-Y4RLpo4uB7pOfikk-tSzvBj_MFbVL2cDq7vaGV72zT75HN2rYR99dzl9ydnd6enGdXP79fnMyuMieBD1nhwAKWZV3zUtRapzdRVaWVqhBCK8gFoHaSO8UT5xBkMa0UJtgVumS12CXfVt7lWHZYOeyHYFuzDE1nw1_jbWM-Jn2zMHP_x-TTvCj0NAkO1oLgn0aMg-ma6LBtbY9-jAa0UlwIzlVCD1eoCz7GgPXbGWDmpQ-T-jDrPhL95f1nb-xrAQn4ugL8uPyv6R-ZkJPc</recordid><startdate>20180109</startdate><enddate>20180109</enddate><creator>Klein, Brianna J</creator><creator>Ahmad, Salar</creator><creator>Vann, Kendra R</creator><creator>Andrews, Forest H</creator><creator>Mayo, Zachary A</creator><creator>Bourriquen, Gaelle</creator><creator>Bridgers, Joseph B</creator><creator>Zhang, Jinyong</creator><creator>Strahl, Brian D</creator><creator>Côté, Jacques</creator><creator>Kutateladze, Tatiana G</creator><general>Oxford University Press</general><scope>TOX</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>5PM</scope></search><sort><creationdate>20180109</creationdate><title>Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain</title><author>Klein, Brianna J ; Ahmad, Salar ; Vann, Kendra R ; Andrews, Forest H ; Mayo, Zachary A ; Bourriquen, Gaelle ; Bridgers, Joseph B ; Zhang, Jinyong ; Strahl, Brian D ; Côté, Jacques ; Kutateladze, Tatiana G</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c412t-8c1a1ebbff2b3f99014e6dba46833961531e9c42c62a1ece1487d6e2b3c89b0f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Acetylation</topic><topic>Adenosine Triphosphatases - chemistry</topic><topic>Adenosine Triphosphatases - genetics</topic><topic>Adenosine Triphosphatases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Binding Sites - genetics</topic><topic>Histone Acetyltransferases - chemistry</topic><topic>Histone Acetyltransferases - genetics</topic><topic>Histone Acetyltransferases - metabolism</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - genetics</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Protein Domains</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><topic>Structural Biology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Klein, Brianna J</creatorcontrib><creatorcontrib>Ahmad, Salar</creatorcontrib><creatorcontrib>Vann, Kendra R</creatorcontrib><creatorcontrib>Andrews, Forest H</creatorcontrib><creatorcontrib>Mayo, Zachary A</creatorcontrib><creatorcontrib>Bourriquen, Gaelle</creatorcontrib><creatorcontrib>Bridgers, Joseph B</creatorcontrib><creatorcontrib>Zhang, Jinyong</creatorcontrib><creatorcontrib>Strahl, Brian D</creatorcontrib><creatorcontrib>Côté, Jacques</creatorcontrib><creatorcontrib>Kutateladze, Tatiana G</creatorcontrib><collection>Oxford Journals Open Access Collection</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Nucleic acids research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Klein, Brianna J</au><au>Ahmad, Salar</au><au>Vann, Kendra R</au><au>Andrews, Forest H</au><au>Mayo, Zachary A</au><au>Bourriquen, Gaelle</au><au>Bridgers, Joseph B</au><au>Zhang, Jinyong</au><au>Strahl, Brian D</au><au>Côté, Jacques</au><au>Kutateladze, Tatiana G</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2018-01-09</date><risdate>2018</risdate><volume>46</volume><issue>1</issue><spage>421</spage><epage>430</epage><pages>421-430</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Abstract
Yaf9 is an integral part of the NuA4 acetyltransferase and the SWR1 chromatin remodeling complexes. Here, we show that Yaf9 associates with acetylated histone H3 with high preference for H3K27ac. The crystal structure of the Yaf9 YEATS domain bound to the H3K27ac peptide reveals that the sequence C-terminal to K27ac stabilizes the complex. The side chain of K27ac inserts between two aromatic residues, mutation of which abrogates the interaction in vitro and leads in vivo to phenotypes similar to YAF9 deletion, including loss of SWR1-dependent incorporation of variant histone H2A.Z. Our findings reveal the molecular basis for the recognition of H3K27ac by a YEATS reader and underscore the importance of this interaction in mediating Yaf9 function within the NuA4 and SWR1 complexes.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>29145630</pmid><doi>10.1093/nar/gkx1151</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Acetylation Adenosine Triphosphatases - chemistry Adenosine Triphosphatases - genetics Adenosine Triphosphatases - metabolism Amino Acid Sequence Binding Sites - genetics Histone Acetyltransferases - chemistry Histone Acetyltransferases - genetics Histone Acetyltransferases - metabolism Histones - chemistry Histones - metabolism Multiprotein Complexes - chemistry Multiprotein Complexes - genetics Multiprotein Complexes - metabolism Protein Domains Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid Structural Biology |
| title | Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain |
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