Guiding the HBO1 complex function through the JADE subunit
JADE is a core subunit of the HBO1 acetyltransferase complex that regulates developmental and epigenetic programs and promotes gene transcription. Here we describe the mechanism by which JADE facilitates recruitment of the HBO1 complex to chromatin and mediates its enzymatic activity. Structural, ge...
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| Veröffentlicht in: | Nature structural & molecular biology 2024-07, Vol.31 (7), p.1039-1049 |
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| creator | Gaurav, Nitika Kanai, Akinori Lachance, Catherine Cox, Khan L. Liu, Jiuyang Grzybowski, Adrian T. Saksouk, Nehmé Klein, Brianna J. Komata, Yosuke Asada, Shuhei Ruthenburg, Alexander J. Poirier, Michael G. Côté, Jacques Yokoyama, Akihiko Kutateladze, Tatiana G. |
| description | JADE is a core subunit of the HBO1 acetyltransferase complex that regulates developmental and epigenetic programs and promotes gene transcription. Here we describe the mechanism by which JADE facilitates recruitment of the HBO1 complex to chromatin and mediates its enzymatic activity. Structural, genomic and complex assembly in vivo studies show that the PZP (PHD1–zinc-knuckle–PHD2) domain of JADE engages the nucleosome through binding to histone H3 and DNA and is necessary for the association with chromatin targets. Recognition of unmethylated H3K4 by PZP directs enzymatic activity of the complex toward histone H4 acetylation, whereas H3K4 hypermethylation alters histone substrate selectivity. We demonstrate that PZP contributes to leukemogenesis, augmenting transforming activity of the NUP98–JADE2 fusion. Our findings highlight biological consequences and the impact of the intact JADE subunit on genomic recruitment, enzymatic function and pathological activity of the HBO1 complex.
JADE is a subunit of human acetyltransferase complex HBO1 that is essential in transcriptional regulation. Gaurav et al. characterize the molecular mechanism by which JADE mediates genomic association and enzymatic and pathological activities of the HBO1 complex. |
| doi_str_mv | 10.1038/s41594-024-01245-2 |
| format | Article |
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JADE is a subunit of human acetyltransferase complex HBO1 that is essential in transcriptional regulation. Gaurav et al. characterize the molecular mechanism by which JADE mediates genomic association and enzymatic and pathological activities of the HBO1 complex.</description><identifier>ISSN: 1545-9993</identifier><identifier>ISSN: 1545-9985</identifier><identifier>EISSN: 1545-9985</identifier><identifier>DOI: 10.1038/s41594-024-01245-2</identifier><identifier>PMID: 38448574</identifier><language>eng</language><publisher>New York: Nature Publishing Group US</publisher><subject>101/6 ; 631/208/176 ; 631/337/100/1701 ; 631/337/100/2285 ; 631/535/1266 ; 631/535/878 ; 82/80 ; 82/83 ; Acetylation ; Acetyltransferase ; Activity recognition ; Animals ; Biochemistry ; Biological activity ; Biological Microscopy ; Biomedical and Life Sciences ; Cancer ; Cell cycle ; Chromatin - metabolism ; Chromatin remodeling ; Enzymatic activity ; Enzymes ; Epigenetics ; Gene regulation ; Genomics ; Histone Acetyltransferases - genetics ; Histone Acetyltransferases - metabolism ; Histone H3 ; Histone H4 ; Histones ; Histones - metabolism ; Homeodomain Proteins ; Humans ; In vivo methods and tests ; Leukemogenesis ; Life Sciences ; Medical research ; Membrane Biology ; Methylation ; Mice ; Models, Molecular ; Molecular biology ; Molecular modelling ; Nucleosomes - metabolism ; Oncology ; Protein Binding ; Protein Domains ; Protein Structure ; Proteins ; RNA polymerase ; Substrates ; Tumor Suppressor Proteins ; Yeast</subject><ispartof>Nature structural & molecular biology, 2024-07, Vol.31 (7), p.1039-1049</ispartof><rights>The Author(s), under exclusive licence to Springer Nature America, Inc. 2024. Springer Nature or its licensor (e.g. a society or other partner) holds exclusive rights to this article under a publishing agreement with the author(s) or other rightsholder(s); author self-archiving of the accepted manuscript version of this article is solely governed by the terms of such publishing agreement and applicable law.</rights><rights>2024. The Author(s), under exclusive licence to Springer Nature America, Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c375t-cfe90306a7f59b81d7e9260cae982380a8463790c9338781b6c26f0c196b55333</citedby><cites>FETCH-LOGICAL-c375t-cfe90306a7f59b81d7e9260cae982380a8463790c9338781b6c26f0c196b55333</cites><orcidid>0000-0001-6116-7996 ; 0000-0001-7375-6990 ; 0000-0003-1555-6768 ; 0000-0002-7340-9603 ; 0000-0002-5639-8068 ; 0000-0003-2709-4564 ; 0000-0001-6751-555X</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/s41594-024-01245-2$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/s41594-024-01245-2$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/38448574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gaurav, Nitika</creatorcontrib><creatorcontrib>Kanai, Akinori</creatorcontrib><creatorcontrib>Lachance, Catherine</creatorcontrib><creatorcontrib>Cox, Khan L.</creatorcontrib><creatorcontrib>Liu, Jiuyang</creatorcontrib><creatorcontrib>Grzybowski, Adrian T.</creatorcontrib><creatorcontrib>Saksouk, Nehmé</creatorcontrib><creatorcontrib>Klein, Brianna J.</creatorcontrib><creatorcontrib>Komata, Yosuke</creatorcontrib><creatorcontrib>Asada, Shuhei</creatorcontrib><creatorcontrib>Ruthenburg, Alexander J.</creatorcontrib><creatorcontrib>Poirier, Michael G.</creatorcontrib><creatorcontrib>Côté, Jacques</creatorcontrib><creatorcontrib>Yokoyama, Akihiko</creatorcontrib><creatorcontrib>Kutateladze, Tatiana G.</creatorcontrib><title>Guiding the HBO1 complex function through the JADE subunit</title><title>Nature structural & molecular biology</title><addtitle>Nat Struct Mol Biol</addtitle><addtitle>Nat Struct Mol Biol</addtitle><description>JADE is a core subunit of the HBO1 acetyltransferase complex that regulates developmental and epigenetic programs and promotes gene transcription. Here we describe the mechanism by which JADE facilitates recruitment of the HBO1 complex to chromatin and mediates its enzymatic activity. Structural, genomic and complex assembly in vivo studies show that the PZP (PHD1–zinc-knuckle–PHD2) domain of JADE engages the nucleosome through binding to histone H3 and DNA and is necessary for the association with chromatin targets. Recognition of unmethylated H3K4 by PZP directs enzymatic activity of the complex toward histone H4 acetylation, whereas H3K4 hypermethylation alters histone substrate selectivity. We demonstrate that PZP contributes to leukemogenesis, augmenting transforming activity of the NUP98–JADE2 fusion. Our findings highlight biological consequences and the impact of the intact JADE subunit on genomic recruitment, enzymatic function and pathological activity of the HBO1 complex.
JADE is a subunit of human acetyltransferase complex HBO1 that is essential in transcriptional regulation. Gaurav et al. characterize the molecular mechanism by which JADE mediates genomic association and enzymatic and pathological activities of the HBO1 complex.</description><subject>101/6</subject><subject>631/208/176</subject><subject>631/337/100/1701</subject><subject>631/337/100/2285</subject><subject>631/535/1266</subject><subject>631/535/878</subject><subject>82/80</subject><subject>82/83</subject><subject>Acetylation</subject><subject>Acetyltransferase</subject><subject>Activity recognition</subject><subject>Animals</subject><subject>Biochemistry</subject><subject>Biological activity</subject><subject>Biological Microscopy</subject><subject>Biomedical and Life Sciences</subject><subject>Cancer</subject><subject>Cell cycle</subject><subject>Chromatin - metabolism</subject><subject>Chromatin remodeling</subject><subject>Enzymatic activity</subject><subject>Enzymes</subject><subject>Epigenetics</subject><subject>Gene regulation</subject><subject>Genomics</subject><subject>Histone Acetyltransferases - 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Academic</collection><jtitle>Nature structural & molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gaurav, Nitika</au><au>Kanai, Akinori</au><au>Lachance, Catherine</au><au>Cox, Khan L.</au><au>Liu, Jiuyang</au><au>Grzybowski, Adrian T.</au><au>Saksouk, Nehmé</au><au>Klein, Brianna J.</au><au>Komata, Yosuke</au><au>Asada, Shuhei</au><au>Ruthenburg, Alexander J.</au><au>Poirier, Michael G.</au><au>Côté, Jacques</au><au>Yokoyama, Akihiko</au><au>Kutateladze, Tatiana G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Guiding the HBO1 complex function through the JADE subunit</atitle><jtitle>Nature structural & molecular biology</jtitle><stitle>Nat Struct Mol Biol</stitle><addtitle>Nat Struct Mol Biol</addtitle><date>2024-07-01</date><risdate>2024</risdate><volume>31</volume><issue>7</issue><spage>1039</spage><epage>1049</epage><pages>1039-1049</pages><issn>1545-9993</issn><issn>1545-9985</issn><eissn>1545-9985</eissn><abstract>JADE is a core subunit of the HBO1 acetyltransferase complex that regulates developmental and epigenetic programs and promotes gene transcription. Here we describe the mechanism by which JADE facilitates recruitment of the HBO1 complex to chromatin and mediates its enzymatic activity. Structural, genomic and complex assembly in vivo studies show that the PZP (PHD1–zinc-knuckle–PHD2) domain of JADE engages the nucleosome through binding to histone H3 and DNA and is necessary for the association with chromatin targets. Recognition of unmethylated H3K4 by PZP directs enzymatic activity of the complex toward histone H4 acetylation, whereas H3K4 hypermethylation alters histone substrate selectivity. We demonstrate that PZP contributes to leukemogenesis, augmenting transforming activity of the NUP98–JADE2 fusion. Our findings highlight biological consequences and the impact of the intact JADE subunit on genomic recruitment, enzymatic function and pathological activity of the HBO1 complex.
JADE is a subunit of human acetyltransferase complex HBO1 that is essential in transcriptional regulation. Gaurav et al. characterize the molecular mechanism by which JADE mediates genomic association and enzymatic and pathological activities of the HBO1 complex.</abstract><cop>New York</cop><pub>Nature Publishing Group US</pub><pmid>38448574</pmid><doi>10.1038/s41594-024-01245-2</doi><tpages>11</tpages><orcidid>https://orcid.org/0000-0001-6116-7996</orcidid><orcidid>https://orcid.org/0000-0001-7375-6990</orcidid><orcidid>https://orcid.org/0000-0003-1555-6768</orcidid><orcidid>https://orcid.org/0000-0002-7340-9603</orcidid><orcidid>https://orcid.org/0000-0002-5639-8068</orcidid><orcidid>https://orcid.org/0000-0003-2709-4564</orcidid><orcidid>https://orcid.org/0000-0001-6751-555X</orcidid></addata></record> |
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| subjects | 101/6 631/208/176 631/337/100/1701 631/337/100/2285 631/535/1266 631/535/878 82/80 82/83 Acetylation Acetyltransferase Activity recognition Animals Biochemistry Biological activity Biological Microscopy Biomedical and Life Sciences Cancer Cell cycle Chromatin - metabolism Chromatin remodeling Enzymatic activity Enzymes Epigenetics Gene regulation Genomics Histone Acetyltransferases - genetics Histone Acetyltransferases - metabolism Histone H3 Histone H4 Histones Histones - metabolism Homeodomain Proteins Humans In vivo methods and tests Leukemogenesis Life Sciences Medical research Membrane Biology Methylation Mice Models, Molecular Molecular biology Molecular modelling Nucleosomes - metabolism Oncology Protein Binding Protein Domains Protein Structure Proteins RNA polymerase Substrates Tumor Suppressor Proteins Yeast |
| title | Guiding the HBO1 complex function through the JADE subunit |
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