Molecular Architecture of Yeast Chromatin Assembly Factor 1
Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features o...
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| Veröffentlicht in: | Scientific reports 2016-05, Vol.6 (1), p.26702-26702, Article 26702 |
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| creator | Kim, Daegeun Setiaputra, Dheva Jung, Taeyang Chung, Jaehee Leitner, Alexander Yoon, Jungmin Aebersold, Ruedi Hebert, Hans Yip, Calvin K. Song, Ji-Joon |
| description | Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes. |
| doi_str_mv | 10.1038/srep26702 |
| format | Article |
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CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep26702</identifier><identifier>PMID: 27221973</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>101/28 ; 631/208/176 ; 631/535 ; Chaperones ; Chromatin ; Chromatin Assembly Factor-1 - chemistry ; Chromatin remodeling ; Electron microscopy ; Histone H3 ; Histones ; Humanities and Social Sciences ; Mass spectrometry ; Mass spectroscopy ; multidisciplinary ; Multiprotein Complexes - chemistry ; Protein Structure, Quaternary ; Saccharomyces cerevisiae - chemistry ; Saccharomyces cerevisiae Proteins - chemistry ; Science ; Science (multidisciplinary) ; Structure-Activity Relationship ; Yeasts</subject><ispartof>Scientific reports, 2016-05, Vol.6 (1), p.26702-26702, Article 26702</ispartof><rights>The Author(s) 2016</rights><rights>Copyright Nature Publishing Group May 2016</rights><rights>Copyright © 2016, Macmillan Publishers Limited 2016 Macmillan Publishers Limited</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c514t-7adf82d7e3ba7c0874b8e00d15d18fcd25c3aa14e49c76274924f489290f9cfc3</citedby><cites>FETCH-LOGICAL-c514t-7adf82d7e3ba7c0874b8e00d15d18fcd25c3aa14e49c76274924f489290f9cfc3</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/PMC4879628/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4879628/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,551,724,777,781,861,882,27905,27906,41101,42170,51557,53772,53774</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27221973$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://urn.kb.se/resolve?urn=urn:nbn:se:kth:diva-188727$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:133642869$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Daegeun</creatorcontrib><creatorcontrib>Setiaputra, Dheva</creatorcontrib><creatorcontrib>Jung, Taeyang</creatorcontrib><creatorcontrib>Chung, Jaehee</creatorcontrib><creatorcontrib>Leitner, Alexander</creatorcontrib><creatorcontrib>Yoon, Jungmin</creatorcontrib><creatorcontrib>Aebersold, Ruedi</creatorcontrib><creatorcontrib>Hebert, Hans</creatorcontrib><creatorcontrib>Yip, Calvin K.</creatorcontrib><creatorcontrib>Song, Ji-Joon</creatorcontrib><title>Molecular Architecture of Yeast Chromatin Assembly Factor 1</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Chromatin Assembly Complex 1 (CAF-1) is a major histone chaperone involved in deposition of histone H3 and H4 into nucleosome. CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes.</description><subject>101/28</subject><subject>631/208/176</subject><subject>631/535</subject><subject>Chaperones</subject><subject>Chromatin</subject><subject>Chromatin Assembly Factor-1 - chemistry</subject><subject>Chromatin remodeling</subject><subject>Electron microscopy</subject><subject>Histone H3</subject><subject>Histones</subject><subject>Humanities and Social Sciences</subject><subject>Mass spectrometry</subject><subject>Mass spectroscopy</subject><subject>multidisciplinary</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Protein Structure, Quaternary</subject><subject>Saccharomyces cerevisiae - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Structure-Activity Relationship</subject><subject>Yeasts</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>D8T</sourceid><recordid>eNp9kVFr2zAUhcVoWUvah_2BYdhLV_AmXcuWxKAQ0nUbdOxlG-xJKPJ14ta2Ukle6b-vQrKQbDC96KL76dzDPYS8YvQdo4V8HzyuoBIUXpBToLzMoQA42qtPyHkIdzSdEhRn6iU5AQHAlChOyYevrkM7dsZnU2-XbUQbR4-Za7JfaELMZkvvehPbIZuGgP28e8pujI3OZ-yMHDemC3i-vSfkx83H77PP-e23T19m09vclozHXJi6kVALLOZGWCoFn0uktGZlzWRjayhtYQzjyJUVFQiugDdcKlC0UbaxxYTkG93wiKtxrle-7Y1_0s60evt0nyrUJeWqEv_lr9ufU-38Qt_HpWZSCljzVxs-wT3WFofoTXfw7bAztEu9cL81l0JVIJPAxVbAu4cRQ9R9Gyx2nRnQjUEzoZjgtOQ0oW_-Qu_c6Ie0vuRGyUqUklWJeruhrHchBdzszDCq16nrXeqJfb3vfkf-yTgBl9t1pNawQL838h-1Z0_LtlI</recordid><startdate>20160525</startdate><enddate>20160525</enddate><creator>Kim, Daegeun</creator><creator>Setiaputra, Dheva</creator><creator>Jung, Taeyang</creator><creator>Chung, Jaehee</creator><creator>Leitner, Alexander</creator><creator>Yoon, Jungmin</creator><creator>Aebersold, Ruedi</creator><creator>Hebert, Hans</creator><creator>Yip, Calvin K.</creator><creator>Song, Ji-Joon</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope><scope>ADTPV</scope><scope>AFDQA</scope><scope>AOWAS</scope><scope>D8T</scope><scope>D8V</scope><scope>ZZAVC</scope></search><sort><creationdate>20160525</creationdate><title>Molecular Architecture of Yeast Chromatin Assembly Factor 1</title><author>Kim, Daegeun ; Setiaputra, Dheva ; Jung, Taeyang ; Chung, Jaehee ; Leitner, Alexander ; Yoon, Jungmin ; Aebersold, Ruedi ; Hebert, Hans ; Yip, Calvin K. ; Song, Ji-Joon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c514t-7adf82d7e3ba7c0874b8e00d15d18fcd25c3aa14e49c76274924f489290f9cfc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>101/28</topic><topic>631/208/176</topic><topic>631/535</topic><topic>Chaperones</topic><topic>Chromatin</topic><topic>Chromatin Assembly Factor-1 - 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CAF-1 is composed of three subunits; p150, p60 and p48 for human and Cac1, Cac2 and Cac3 for yeast. Despite of its central role in chromatin formation, structural features of the full CAF-1 in complex with histones and other chaperones have not been well characterized. Here, we dissect molecular architecture of yeast CAF-1 (yCAF-1) by cross-linking mass spectrometry (XL-MS) and negative stain single-particle electron microscopy (EM). Our work revealed that Cac1, the largest subunit of yCAF-1, might serve as a major histone binding platform linking Cac2 and Cac3. In addition, EM analysis showed that yCAF-1 adopts a bilobal shape and Cac1 connecting Cac2 and Cac3 to generate a platform for binding histones. This study provides the first structural glimpse of the full CAF-1 complex and a structural framework to understand histone chaperoning processes.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>27221973</pmid><doi>10.1038/srep26702</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 101/28 631/208/176 631/535 Chaperones Chromatin Chromatin Assembly Factor-1 - chemistry Chromatin remodeling Electron microscopy Histone H3 Histones Humanities and Social Sciences Mass spectrometry Mass spectroscopy multidisciplinary Multiprotein Complexes - chemistry Protein Structure, Quaternary Saccharomyces cerevisiae - chemistry Saccharomyces cerevisiae Proteins - chemistry Science Science (multidisciplinary) Structure-Activity Relationship Yeasts |
| title | Molecular Architecture of Yeast Chromatin Assembly Factor 1 |
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