The fork protection complex recruits FACT to reorganize nucleosomes during replication
Abstract Chromosome replication depends on efficient removal of nucleosomes by accessory factors to ensure rapid access to genomic information. Here, we show this process requires recruitment of the nucleosome reorganization activity of the histone chaperone FACT. Using single-molecule FRET, we demo...
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| Veröffentlicht in: | Nucleic acids research 2022-02, Vol.50 (3), p.1317-1334 |
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| creator | Safaric, Barbara Chacin, Erika Scherr, Matthias J Rajappa, Lional Gebhardt, Christian Kurat, Christoph F Cordes, Thorben Duderstadt, Karl E |
| description | Abstract
Chromosome replication depends on efficient removal of nucleosomes by accessory factors to ensure rapid access to genomic information. Here, we show this process requires recruitment of the nucleosome reorganization activity of the histone chaperone FACT. Using single-molecule FRET, we demonstrate that reorganization of nucleosomal DNA by FACT requires coordinated engagement by the middle and C-terminal domains of Spt16 and Pob3 but does not require the N-terminus of Spt16. Using structure-guided pulldowns, we demonstrate instead that the N-terminal region is critical for recruitment by the fork protection complex subunit Tof1. Using in vitro chromatin replication assays, we confirm the importance of these interactions for robust replication. Our findings support a mechanism in which nucleosomes are removed through the coordinated engagement of multiple FACT domains positioned at the replication fork by the fork protection complex. |
| doi_str_mv | 10.1093/nar/gkac005 |
| format | Article |
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Chromosome replication depends on efficient removal of nucleosomes by accessory factors to ensure rapid access to genomic information. Here, we show this process requires recruitment of the nucleosome reorganization activity of the histone chaperone FACT. Using single-molecule FRET, we demonstrate that reorganization of nucleosomal DNA by FACT requires coordinated engagement by the middle and C-terminal domains of Spt16 and Pob3 but does not require the N-terminus of Spt16. Using structure-guided pulldowns, we demonstrate instead that the N-terminal region is critical for recruitment by the fork protection complex subunit Tof1. Using in vitro chromatin replication assays, we confirm the importance of these interactions for robust replication. Our findings support a mechanism in which nucleosomes are removed through the coordinated engagement of multiple FACT domains positioned at the replication fork by the fork protection complex.</description><identifier>ISSN: 0305-1048</identifier><identifier>EISSN: 1362-4962</identifier><identifier>DOI: 10.1093/nar/gkac005</identifier><identifier>PMID: 35061899</identifier><language>eng</language><publisher>England: Oxford University Press</publisher><subject>Data Resources and Analyses ; DNA Replication ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; High Mobility Group Proteins - metabolism ; Nucleosomes - genetics ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Transcription Factors - genetics ; Transcriptional Elongation Factors - genetics</subject><ispartof>Nucleic acids research, 2022-02, Vol.50 (3), p.1317-1334</ispartof><rights>The Author(s) 2022. Published by Oxford University Press on behalf of Nucleic Acids Research. 2022</rights><rights>The Author(s) 2022. 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-c478t-ac3a5300c64432c97af9b74e24b77d690a36f967b0a5035af37fe0f15fb9d4f13</citedby><cites>FETCH-LOGICAL-c478t-ac3a5300c64432c97af9b74e24b77d690a36f967b0a5035af37fe0f15fb9d4f13</cites><orcidid>0000-0003-0110-3709 ; 0000-0002-6278-191X ; 0000-0002-1279-7841</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8860610/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8860610/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,315,728,781,785,865,886,1605,27926,27927,53793,53795</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/35061899$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Safaric, Barbara</creatorcontrib><creatorcontrib>Chacin, Erika</creatorcontrib><creatorcontrib>Scherr, Matthias J</creatorcontrib><creatorcontrib>Rajappa, Lional</creatorcontrib><creatorcontrib>Gebhardt, Christian</creatorcontrib><creatorcontrib>Kurat, Christoph F</creatorcontrib><creatorcontrib>Cordes, Thorben</creatorcontrib><creatorcontrib>Duderstadt, Karl E</creatorcontrib><title>The fork protection complex recruits FACT to reorganize nucleosomes during replication</title><title>Nucleic acids research</title><addtitle>Nucleic Acids Res</addtitle><description>Abstract
Chromosome replication depends on efficient removal of nucleosomes by accessory factors to ensure rapid access to genomic information. Here, we show this process requires recruitment of the nucleosome reorganization activity of the histone chaperone FACT. Using single-molecule FRET, we demonstrate that reorganization of nucleosomal DNA by FACT requires coordinated engagement by the middle and C-terminal domains of Spt16 and Pob3 but does not require the N-terminus of Spt16. Using structure-guided pulldowns, we demonstrate instead that the N-terminal region is critical for recruitment by the fork protection complex subunit Tof1. Using in vitro chromatin replication assays, we confirm the importance of these interactions for robust replication. Our findings support a mechanism in which nucleosomes are removed through the coordinated engagement of multiple FACT domains positioned at the replication fork by the fork protection complex.</description><subject>Data Resources and Analyses</subject><subject>DNA Replication</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>High Mobility Group Proteins - metabolism</subject><subject>Nucleosomes - genetics</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Transcription Factors - genetics</subject><subject>Transcriptional Elongation Factors - genetics</subject><issn>0305-1048</issn><issn>1362-4962</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><sourceid>TOX</sourceid><sourceid>EIF</sourceid><recordid>eNp9kU1LxDAQhoMo7rp68i49iSDVSZOmyUWQxS9Y8LJ6DWk2WaNtU5NW1F9vZddFL54GZh6eGeZF6BDDGQZBzhsVzpcvSgPkW2iMCctSKli2jcZAIE8xUD5CezE-A2CKc7qLRiQHhrkQY_Q4fzKJ9eElaYPvjO6cbxLt67Yy70kwOvSui8n15XSedH5o-LBUjfs0SdPryvjoaxOTRR9csxymbeW0-lbsox2rqmgO1nWCHq6v5tPbdHZ_cze9nKWaFrxLlSYqJwCaUUoyLQplRVlQk9GyKBZMgCLMClaUoHIgubKksAYszm0pFtRiMkEXK2_bl7VZaNN0QVWyDa5W4UN65eTfSeOe5NK_Sc7Z8AIYBCdrQfCvvYmdrF3UpqpUY3wfZcayLOOcYz6gpytUBx9jMHazBoP8TkIOSch1EgN99PuyDfvz-gE4XgG-b_81fQEUKpTK</recordid><startdate>20220222</startdate><enddate>20220222</enddate><creator>Safaric, Barbara</creator><creator>Chacin, Erika</creator><creator>Scherr, Matthias J</creator><creator>Rajappa, Lional</creator><creator>Gebhardt, Christian</creator><creator>Kurat, Christoph F</creator><creator>Cordes, Thorben</creator><creator>Duderstadt, Karl E</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><orcidid>https://orcid.org/0000-0003-0110-3709</orcidid><orcidid>https://orcid.org/0000-0002-6278-191X</orcidid><orcidid>https://orcid.org/0000-0002-1279-7841</orcidid></search><sort><creationdate>20220222</creationdate><title>The fork protection complex recruits FACT to reorganize nucleosomes during replication</title><author>Safaric, Barbara ; Chacin, Erika ; Scherr, Matthias J ; Rajappa, Lional ; Gebhardt, Christian ; Kurat, Christoph F ; Cordes, Thorben ; Duderstadt, Karl E</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c478t-ac3a5300c64432c97af9b74e24b77d690a36f967b0a5035af37fe0f15fb9d4f13</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Data Resources and Analyses</topic><topic>DNA Replication</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>High Mobility Group Proteins - metabolism</topic><topic>Nucleosomes - genetics</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Transcription Factors - genetics</topic><topic>Transcriptional Elongation Factors - genetics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Safaric, Barbara</creatorcontrib><creatorcontrib>Chacin, Erika</creatorcontrib><creatorcontrib>Scherr, Matthias J</creatorcontrib><creatorcontrib>Rajappa, Lional</creatorcontrib><creatorcontrib>Gebhardt, Christian</creatorcontrib><creatorcontrib>Kurat, Christoph F</creatorcontrib><creatorcontrib>Cordes, Thorben</creatorcontrib><creatorcontrib>Duderstadt, Karl E</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>Safaric, Barbara</au><au>Chacin, Erika</au><au>Scherr, Matthias J</au><au>Rajappa, Lional</au><au>Gebhardt, Christian</au><au>Kurat, Christoph F</au><au>Cordes, Thorben</au><au>Duderstadt, Karl E</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The fork protection complex recruits FACT to reorganize nucleosomes during replication</atitle><jtitle>Nucleic acids research</jtitle><addtitle>Nucleic Acids Res</addtitle><date>2022-02-22</date><risdate>2022</risdate><volume>50</volume><issue>3</issue><spage>1317</spage><epage>1334</epage><pages>1317-1334</pages><issn>0305-1048</issn><eissn>1362-4962</eissn><abstract>Abstract
Chromosome replication depends on efficient removal of nucleosomes by accessory factors to ensure rapid access to genomic information. Here, we show this process requires recruitment of the nucleosome reorganization activity of the histone chaperone FACT. Using single-molecule FRET, we demonstrate that reorganization of nucleosomal DNA by FACT requires coordinated engagement by the middle and C-terminal domains of Spt16 and Pob3 but does not require the N-terminus of Spt16. Using structure-guided pulldowns, we demonstrate instead that the N-terminal region is critical for recruitment by the fork protection complex subunit Tof1. Using in vitro chromatin replication assays, we confirm the importance of these interactions for robust replication. Our findings support a mechanism in which nucleosomes are removed through the coordinated engagement of multiple FACT domains positioned at the replication fork by the fork protection complex.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>35061899</pmid><doi>10.1093/nar/gkac005</doi><tpages>18</tpages><orcidid>https://orcid.org/0000-0003-0110-3709</orcidid><orcidid>https://orcid.org/0000-0002-6278-191X</orcidid><orcidid>https://orcid.org/0000-0002-1279-7841</orcidid><oa>free_for_read</oa></addata></record> |
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| subjects | Data Resources and Analyses DNA Replication DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism High Mobility Group Proteins - metabolism Nucleosomes - genetics Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Transcription Factors - genetics Transcriptional Elongation Factors - genetics |
| title | The fork protection complex recruits FACT to reorganize nucleosomes during replication |
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