Structural and functional analysis of the SET3 histone deacetylase complex
The SET3 complex (SET3C) is a seven‐subunit histone deacetylase complex that is capable of transcriptional regulation. Methylated histone 3 marks recruit SET3C to the nucleosome, and the SET3C catalytic subunits deacetylate the histone 3 and 4 tails. There is very limited structural knowledge of the...
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| Veröffentlicht in: | Acta crystallographica. Section F, Structural biology communications Structural biology communications, 2022-03, Vol.78 (3), p.113-118 |
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| container_title | Acta crystallographica. Section F, Structural biology communications |
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| creator | Reyes, Alexis A. Fishbain, Susan He, Yuan |
| description | The SET3 complex (SET3C) is a seven‐subunit histone deacetylase complex that is capable of transcriptional regulation. Methylated histone 3 marks recruit SET3C to the nucleosome, and the SET3C catalytic subunits deacetylate the histone 3 and 4 tails. There is very limited structural knowledge of the SET3C subunits, with most subunits having unknown structures or functions. Here, a catalytically active SET3 complex was endogenously purified from Saccharomyces cerevisiae and utilized for negative‐stain electron microscopy (EM) to determine an apo model for the holo complex. The negative‐stain EM 3D model revealed a three‐lobe architecture, with each lobe extending from a central point.
An electron‐microscopy model of the SET3 histone deacetylase complex reveals a three‐lobe architecture. |
| doi_str_mv | 10.1107/S2053230X22000553 |
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An electron‐microscopy model of the SET3 histone deacetylase complex reveals a three‐lobe architecture.</description><identifier>ISSN: 2053-230X</identifier><identifier>EISSN: 2053-230X</identifier><identifier>DOI: 10.1107/S2053230X22000553</identifier><identifier>PMID: 35234136</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Catalytic subunits ; Crystallography, X-Ray ; Electron microscopy ; Functional analysis ; Gene regulation ; Histone deacetylase ; Histone Deacetylases - chemistry ; Histone Deacetylases - genetics ; Histone Deacetylases - metabolism ; histone deacetylation ; Histones ; Research Communications ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; SET3 complex ; Structure-Activity Relationship ; Structure-function relationships ; Three dimensional models ; Transcription ; Transcription, Genetic</subject><ispartof>Acta crystallographica. Section F, Structural biology communications, 2022-03, Vol.78 (3), p.113-118</ispartof><rights>2022 Reyes, Fishbain and He. published by IUCr Journals.</rights><rights>Copyright Wiley Subscription Services, Inc. Mar 2022</rights><rights>Reyes, Fishbain and He 2022 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4775-2968783a91bc5e6bfbe2801ef690d77962a3e9295e45b1e20261895285c4b8e73</citedby><cites>FETCH-LOGICAL-c4775-2968783a91bc5e6bfbe2801ef690d77962a3e9295e45b1e20261895285c4b8e73</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/PMC8900736/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8900736/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,725,778,782,883,1414,27907,27908,45557,45558,53774,53776</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35234136$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Reyes, Alexis A.</creatorcontrib><creatorcontrib>Fishbain, Susan</creatorcontrib><creatorcontrib>He, Yuan</creatorcontrib><title>Structural and functional analysis of the SET3 histone deacetylase complex</title><title>Acta crystallographica. Section F, Structural biology communications</title><addtitle>Acta Crystallogr F Struct Biol Commun</addtitle><description>The SET3 complex (SET3C) is a seven‐subunit histone deacetylase complex that is capable of transcriptional regulation. Methylated histone 3 marks recruit SET3C to the nucleosome, and the SET3C catalytic subunits deacetylate the histone 3 and 4 tails. There is very limited structural knowledge of the SET3C subunits, with most subunits having unknown structures or functions. Here, a catalytically active SET3 complex was endogenously purified from Saccharomyces cerevisiae and utilized for negative‐stain electron microscopy (EM) to determine an apo model for the holo complex. The negative‐stain EM 3D model revealed a three‐lobe architecture, with each lobe extending from a central point.
An electron‐microscopy model of the SET3 histone deacetylase complex reveals a three‐lobe architecture.</description><subject>Catalytic subunits</subject><subject>Crystallography, X-Ray</subject><subject>Electron microscopy</subject><subject>Functional analysis</subject><subject>Gene regulation</subject><subject>Histone deacetylase</subject><subject>Histone Deacetylases - chemistry</subject><subject>Histone Deacetylases - genetics</subject><subject>Histone Deacetylases - metabolism</subject><subject>histone deacetylation</subject><subject>Histones</subject><subject>Research Communications</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>SET3 complex</subject><subject>Structure-Activity Relationship</subject><subject>Structure-function relationships</subject><subject>Three dimensional models</subject><subject>Transcription</subject><subject>Transcription, Genetic</subject><issn>2053-230X</issn><issn>2053-230X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtPAjEUhRujUYL8ADdmEjdu0D6m7XRjQgj4TFyAia6aTrkjQ4YpTmdU_r1F0KAuXLW9_c7JvecidETwGSFYno8o5owy_EgpxphztoNaq1J3Vdvduh-gjvezwKxkRKp9dMA4ZTFhooVuRnXV2LqpTBGZchJlTWnr3JWfT1Msfe4jl0X1FKLRYMyiae5rV0I0AWOhXhbGQ2TdfFHA-yHay0zhobM52-hhOBj3r7p395fX_d5d18ZS8i5VIpEJM4qkloNIsxRogglkQuGJlEpQw0BRxSHmKQGKqSCJ4jThNk4TkKyNLta-iyadw8RCWYfu9aLK56Zaamdy_fOnzKf62b3qRGEsmQgGpxuDyr004Gs9z72FojAluMZrKkI-sQgRBfTkFzpzTRWC-aSEVCoWPFBkTdnKeV9B9t0MwXqVuv6zrKA53p7iW_G1mgCoNfCWF7D831H3noZ0cMsx5ewDtdaegQ</recordid><startdate>202203</startdate><enddate>202203</enddate><creator>Reyes, Alexis A.</creator><creator>Fishbain, Susan</creator><creator>He, Yuan</creator><general>International Union of Crystallography</general><general>Wiley Subscription Services, Inc</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>7QL</scope><scope>7T7</scope><scope>7TM</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>202203</creationdate><title>Structural and functional analysis of the SET3 histone deacetylase complex</title><author>Reyes, Alexis A. ; Fishbain, Susan ; He, Yuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4775-2968783a91bc5e6bfbe2801ef690d77962a3e9295e45b1e20261895285c4b8e73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Catalytic subunits</topic><topic>Crystallography, X-Ray</topic><topic>Electron microscopy</topic><topic>Functional analysis</topic><topic>Gene regulation</topic><topic>Histone deacetylase</topic><topic>Histone Deacetylases - chemistry</topic><topic>Histone Deacetylases - genetics</topic><topic>Histone Deacetylases - metabolism</topic><topic>histone deacetylation</topic><topic>Histones</topic><topic>Research Communications</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>SET3 complex</topic><topic>Structure-Activity Relationship</topic><topic>Structure-function relationships</topic><topic>Three dimensional models</topic><topic>Transcription</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Reyes, Alexis A.</creatorcontrib><creatorcontrib>Fishbain, Susan</creatorcontrib><creatorcontrib>He, Yuan</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids 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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Acta crystallographica. 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There is very limited structural knowledge of the SET3C subunits, with most subunits having unknown structures or functions. Here, a catalytically active SET3 complex was endogenously purified from Saccharomyces cerevisiae and utilized for negative‐stain electron microscopy (EM) to determine an apo model for the holo complex. The negative‐stain EM 3D model revealed a three‐lobe architecture, with each lobe extending from a central point.
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| subjects | Catalytic subunits Crystallography, X-Ray Electron microscopy Functional analysis Gene regulation Histone deacetylase Histone Deacetylases - chemistry Histone Deacetylases - genetics Histone Deacetylases - metabolism histone deacetylation Histones Research Communications Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism SET3 complex Structure-Activity Relationship Structure-function relationships Three dimensional models Transcription Transcription, Genetic |
| title | Structural and functional analysis of the SET3 histone deacetylase complex |
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