Replication-Independent Histone Deposition by the HIR Complex and Asf1
The orderly deposition of histones onto DNA is mediated by conserved assembly complexes, including chromatin assembly factor-1 (CAF-1) and the Hir proteins [1–4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo [5, 6]. The Hir proteins...
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| Veröffentlicht in: | Current biology 2005-11, Vol.15 (22), p.2044-2049 |
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| creator | Green, Erin M. Antczak, Andrew J. Bailey, Aaron O. Franco, Alexa A. Wu, Kevin J. Yates, John R. Kaufman, Paul D. |
| description | The orderly deposition of histones onto DNA is mediated by conserved assembly complexes, including chromatin assembly factor-1 (CAF-1) and the Hir proteins
[1–4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo
[5, 6]. The Hir proteins and CAF-1 share a common partner, the highly conserved histone H3/H4 binding protein Asf1, which binds the middle subunit of CAF-1 as well as to Hir proteins
[7–11]. Asf1 binds to newly synthesized histones H3/H4
[12], and this complex stimulates histone deposition by CAF-1
[7, 11, 12]. In yeast, Asf1 is required for the contribution of the Hir proteins to gene silencing
[7, 13]. Here, we demonstrate that Hir1, Hir2, Hir3, and Hpc2 comprise the HIR complex, which copurifies with the histone deposition protein Asf1. Together, the HIR complex and Asf1 deposit histones onto DNA in a replication-independent manner. Histone deposition by the HIR complex and Asf1 is impaired by a mutation in Asf1 that inhibits HIR binding. These data indicate that the HIR complex and Asf1 proteins function together as a conserved eukaryotic pathway for histone replacement throughout the cell cycle. |
| doi_str_mv | 10.1016/j.cub.2005.10.053 |
| format | Article |
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[1–4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo
[5, 6]. The Hir proteins and CAF-1 share a common partner, the highly conserved histone H3/H4 binding protein Asf1, which binds the middle subunit of CAF-1 as well as to Hir proteins
[7–11]. Asf1 binds to newly synthesized histones H3/H4
[12], and this complex stimulates histone deposition by CAF-1
[7, 11, 12]. In yeast, Asf1 is required for the contribution of the Hir proteins to gene silencing
[7, 13]. Here, we demonstrate that Hir1, Hir2, Hir3, and Hpc2 comprise the HIR complex, which copurifies with the histone deposition protein Asf1. Together, the HIR complex and Asf1 deposit histones onto DNA in a replication-independent manner. Histone deposition by the HIR complex and Asf1 is impaired by a mutation in Asf1 that inhibits HIR binding. These data indicate that the HIR complex and Asf1 proteins function together as a conserved eukaryotic pathway for histone replacement throughout the cell cycle.</description><identifier>ISSN: 0960-9822</identifier><identifier>EISSN: 1879-0445</identifier><identifier>DOI: 10.1016/j.cub.2005.10.053</identifier><identifier>PMID: 16303565</identifier><language>eng</language><publisher>England: Elsevier Inc</publisher><subject>Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Chromatin Assembly Factor-1 ; Chromatin Immunoprecipitation ; Chromosomal Proteins, Non-Histone - metabolism ; DNA - metabolism ; DNA-Binding Proteins - metabolism ; Electrophoretic Mobility Shift Assay ; Histones - metabolism ; Immunoblotting ; Mass Spectrometry ; Molecular Chaperones ; Multiprotein Complexes - metabolism ; Mutation - genetics ; Nuclear Proteins - metabolism ; Repressor Proteins - metabolism ; Saccharomyces cerevisiae Proteins - genetics ; Saccharomyces cerevisiae Proteins - metabolism ; Yeasts</subject><ispartof>Current biology, 2005-11, Vol.15 (22), p.2044-2049</ispartof><rights>2005 Elsevier Ltd</rights><rights>2009 Elsevier Inc. All rights reserved 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c480t-ea045b9be9485e0c684423614d12856c195482985d081a6fc6c9c8c0bb2355dc3</citedby><cites>FETCH-LOGICAL-c480t-ea045b9be9485e0c684423614d12856c195482985d081a6fc6c9c8c0bb2355dc3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0960982205013060$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65534</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16303565$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Green, Erin M.</creatorcontrib><creatorcontrib>Antczak, Andrew J.</creatorcontrib><creatorcontrib>Bailey, Aaron O.</creatorcontrib><creatorcontrib>Franco, Alexa A.</creatorcontrib><creatorcontrib>Wu, Kevin J.</creatorcontrib><creatorcontrib>Yates, John R.</creatorcontrib><creatorcontrib>Kaufman, Paul D.</creatorcontrib><title>Replication-Independent Histone Deposition by the HIR Complex and Asf1</title><title>Current biology</title><addtitle>Curr Biol</addtitle><description>The orderly deposition of histones onto DNA is mediated by conserved assembly complexes, including chromatin assembly factor-1 (CAF-1) and the Hir proteins
[1–4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo
[5, 6]. The Hir proteins and CAF-1 share a common partner, the highly conserved histone H3/H4 binding protein Asf1, which binds the middle subunit of CAF-1 as well as to Hir proteins
[7–11]. Asf1 binds to newly synthesized histones H3/H4
[12], and this complex stimulates histone deposition by CAF-1
[7, 11, 12]. In yeast, Asf1 is required for the contribution of the Hir proteins to gene silencing
[7, 13]. Here, we demonstrate that Hir1, Hir2, Hir3, and Hpc2 comprise the HIR complex, which copurifies with the histone deposition protein Asf1. Together, the HIR complex and Asf1 deposit histones onto DNA in a replication-independent manner. Histone deposition by the HIR complex and Asf1 is impaired by a mutation in Asf1 that inhibits HIR binding. These data indicate that the HIR complex and Asf1 proteins function together as a conserved eukaryotic pathway for histone replacement throughout the cell cycle.</description><subject>Cell Cycle Proteins - genetics</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Chromatin Assembly Factor-1</subject><subject>Chromatin Immunoprecipitation</subject><subject>Chromosomal Proteins, Non-Histone - metabolism</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Electrophoretic Mobility Shift Assay</subject><subject>Histones - metabolism</subject><subject>Immunoblotting</subject><subject>Mass Spectrometry</subject><subject>Molecular Chaperones</subject><subject>Multiprotein Complexes - metabolism</subject><subject>Mutation - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>Repressor Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - genetics</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Yeasts</subject><issn>0960-9822</issn><issn>1879-0445</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkVtLAzEQhYMoWi8_wBfZJ9-2TrJJmiAIUi8tCILoc8hmp5qy3aybrei_N6XFy4u-ZEjmm8PJHEKOKQwpUHk2H7plOWQAIt2HIIotMqBqpHPgXGyTAWgJuVaM7ZH9GOcAlCktd8kelQUUQooBuXnAtvbO9j40-bSpsMV0NH028bEPDWZX2IboV-2s_Mj6F8wm04dsHBZtje-ZbarsMs7oIdmZ2Tri0aYekKeb68fxJL-7v52OL-9yxxX0OVrgotQlaq4EgpOKc1ZIyqvkTEhHteCKaSUqUNTKmZNOO-WgLFkhROWKA3Kx1m2X5QIrl5x2tjZt5xe2-zDBevO70_gX8xzeDFNUKyqSwOlGoAuvS4y9WfjosK5tg2EZjVSK0RHl_4IJAjWSMoF0DbouxNjh7MsNBbOKycxNismsYlo9pZjSzMnPb3xPbHJJwPkawLTMN4-dic5j47DyHbreVMH_If8JibGiQQ</recordid><startdate>20051122</startdate><enddate>20051122</enddate><creator>Green, Erin M.</creator><creator>Antczak, Andrew J.</creator><creator>Bailey, Aaron O.</creator><creator>Franco, Alexa A.</creator><creator>Wu, Kevin J.</creator><creator>Yates, John R.</creator><creator>Kaufman, Paul D.</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>7TM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20051122</creationdate><title>Replication-Independent Histone Deposition by the HIR Complex and Asf1</title><author>Green, Erin M. ; Antczak, Andrew J. ; Bailey, Aaron O. ; Franco, Alexa A. ; Wu, Kevin J. ; Yates, John R. ; Kaufman, Paul D.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c480t-ea045b9be9485e0c684423614d12856c195482985d081a6fc6c9c8c0bb2355dc3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Cell Cycle Proteins - genetics</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Chromatin Assembly Factor-1</topic><topic>Chromatin Immunoprecipitation</topic><topic>Chromosomal Proteins, Non-Histone - metabolism</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoretic Mobility Shift Assay</topic><topic>Histones - metabolism</topic><topic>Immunoblotting</topic><topic>Mass Spectrometry</topic><topic>Molecular Chaperones</topic><topic>Multiprotein Complexes - metabolism</topic><topic>Mutation - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>Repressor Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - genetics</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Green, Erin M.</creatorcontrib><creatorcontrib>Antczak, Andrew J.</creatorcontrib><creatorcontrib>Bailey, Aaron O.</creatorcontrib><creatorcontrib>Franco, Alexa A.</creatorcontrib><creatorcontrib>Wu, Kevin J.</creatorcontrib><creatorcontrib>Yates, John R.</creatorcontrib><creatorcontrib>Kaufman, Paul D.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Current biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Green, Erin M.</au><au>Antczak, Andrew J.</au><au>Bailey, Aaron O.</au><au>Franco, Alexa A.</au><au>Wu, Kevin J.</au><au>Yates, John R.</au><au>Kaufman, Paul D.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Replication-Independent Histone Deposition by the HIR Complex and Asf1</atitle><jtitle>Current biology</jtitle><addtitle>Curr Biol</addtitle><date>2005-11-22</date><risdate>2005</risdate><volume>15</volume><issue>22</issue><spage>2044</spage><epage>2049</epage><pages>2044-2049</pages><issn>0960-9822</issn><eissn>1879-0445</eissn><abstract>The orderly deposition of histones onto DNA is mediated by conserved assembly complexes, including chromatin assembly factor-1 (CAF-1) and the Hir proteins
[1–4]. CAF-1 and the Hir proteins operate in distinct but functionally overlapping histone deposition pathways in vivo
[5, 6]. The Hir proteins and CAF-1 share a common partner, the highly conserved histone H3/H4 binding protein Asf1, which binds the middle subunit of CAF-1 as well as to Hir proteins
[7–11]. Asf1 binds to newly synthesized histones H3/H4
[12], and this complex stimulates histone deposition by CAF-1
[7, 11, 12]. In yeast, Asf1 is required for the contribution of the Hir proteins to gene silencing
[7, 13]. Here, we demonstrate that Hir1, Hir2, Hir3, and Hpc2 comprise the HIR complex, which copurifies with the histone deposition protein Asf1. Together, the HIR complex and Asf1 deposit histones onto DNA in a replication-independent manner. Histone deposition by the HIR complex and Asf1 is impaired by a mutation in Asf1 that inhibits HIR binding. These data indicate that the HIR complex and Asf1 proteins function together as a conserved eukaryotic pathway for histone replacement throughout the cell cycle.</abstract><cop>England</cop><pub>Elsevier Inc</pub><pmid>16303565</pmid><doi>10.1016/j.cub.2005.10.053</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; Cell Press Free Archives; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Cell Cycle Proteins - genetics Cell Cycle Proteins - metabolism Chromatin Assembly Factor-1 Chromatin Immunoprecipitation Chromosomal Proteins, Non-Histone - metabolism DNA - metabolism DNA-Binding Proteins - metabolism Electrophoretic Mobility Shift Assay Histones - metabolism Immunoblotting Mass Spectrometry Molecular Chaperones Multiprotein Complexes - metabolism Mutation - genetics Nuclear Proteins - metabolism Repressor Proteins - metabolism Saccharomyces cerevisiae Proteins - genetics Saccharomyces cerevisiae Proteins - metabolism Yeasts |
| title | Replication-Independent Histone Deposition by the HIR Complex and Asf1 |
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