Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications
Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface...
Gespeichert in:
| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-04, Vol.102 (17), p.5975-5980 |
|---|---|
| Hauptverfasser: | , , , , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 5980 |
|---|---|
| container_issue | 17 |
| container_start_page | 5975 |
| container_title | Proceedings of the National Academy of Sciences - PNAS |
| container_volume | 102 |
| creator | Mousson, Florence Lautrette, Aurélie Thuret, Jean-Yves Agez, Morgane Courbeyrette, Régis Amigues, Béatrice Becker, Emmanuelle Neumann, Jean-Michel Guerois, Raphaël Mann, Carl Ochsenbein, Françoise Felsenfeld, Gary |
| description | Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing. |
| doi_str_mv | 10.1073/pnas.0500149102 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmed_primary_15840725</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>3375238</jstor_id><sourcerecordid>3375238</sourcerecordid><originalsourceid>FETCH-LOGICAL-c561t-c78628d7f925b95e52ba43a93dca2d4a63ef67d3ef4b8343dbfa6f50925417543</originalsourceid><addsrcrecordid>eNp90c1v0zAYBnALgVgZnLkgsDggOGR7_RU7F6QyMVqpEgfghmS5jk1TpXGxnQH_PQ6tVtiBS6wov_dx7AehpwQuCEh2uR9MugABQHhDgN5DMwINqWrewH00A6CyUpzyM_QopS0ANELBQ3RGhOIgqZihr59yHG0eo-nxO5O6hH2IOG8cXg7ZRWNzFwYcPJ4nT_CPLm_woks5DA4vGDZDi5c54etx-ANLyHK37ztrprf0GD3wpk_uyXE9R1-u33--WlSrjx-WV_NVZUVNcmWlqqlqpW-oWDfCCbo2nJmGtdbQlpuaOV_Ltjz5WjHO2rU3tRdQOCdScHaO3h5y9-N651rrhlzOo_ex25n4SwfT6X-_DN1Gfws3moCSDYUS8OYQsLkztpivtHVGA5GccypvSLGvjpvF8H10Ketdl6zrezO4MCZNpJJEgCrw5R24DWMsd5Q0BcLqmlFW0OUB2RhSis7fbk9ATxXrqWJ9qrhMPP_7sCd_7LSAF0cwTZ7iaPk1LRo5idf_F9qPfZ_dz1zoswPdltLjrWVMCsoU-w3-E8Le</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>201366323</pqid></control><display><type>article</type><title>Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><source>Free Full-Text Journals in Chemistry</source><creator>Mousson, Florence ; Lautrette, Aurélie ; Thuret, Jean-Yves ; Agez, Morgane ; Courbeyrette, Régis ; Amigues, Béatrice ; Becker, Emmanuelle ; Neumann, Jean-Michel ; Guerois, Raphaël ; Mann, Carl ; Ochsenbein, Françoise ; Felsenfeld, Gary</creator><creatorcontrib>Mousson, Florence ; Lautrette, Aurélie ; Thuret, Jean-Yves ; Agez, Morgane ; Courbeyrette, Régis ; Amigues, Béatrice ; Becker, Emmanuelle ; Neumann, Jean-Michel ; Guerois, Raphaël ; Mann, Carl ; Ochsenbein, Françoise ; Felsenfeld, Gary</creatorcontrib><description>Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0500149102</identifier><identifier>PMID: 15840725</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Animals ; Binding Sites ; Biochemistry, Molecular Biology ; Biological Sciences ; Biophysics ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; Chemical equilibrium ; Chickens ; DNA ; DNA damage ; DNA repair ; Genetic mutation ; Glutathione Transferase - chemistry ; Glutathione Transferase - metabolism ; Histones ; Histones - chemistry ; Histones - metabolism ; Humans ; Life Sciences ; Magnetic Resonance Spectroscopy ; Models, Molecular ; Mutagenesis, Site-Directed ; Mutation ; Nucleosomes ; Phenotypes ; Plasmids ; Protein Conformation ; Protein Structure, Secondary ; Proteins ; Recombinant Fusion Proteins - chemistry ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-04, Vol.102 (17), p.5975-5980</ispartof><rights>Copyright 1993/2005 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Apr 26, 2005</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><rights>Copyright © 2005, The National Academy of Sciences 2005</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c561t-c78628d7f925b95e52ba43a93dca2d4a63ef67d3ef4b8343dbfa6f50925417543</citedby><cites>FETCH-LOGICAL-c561t-c78628d7f925b95e52ba43a93dca2d4a63ef67d3ef4b8343dbfa6f50925417543</cites><orcidid>0000-0002-7673-0582</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/17.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3375238$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3375238$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15840725$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://cea.hal.science/cea-01744427$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Mousson, Florence</creatorcontrib><creatorcontrib>Lautrette, Aurélie</creatorcontrib><creatorcontrib>Thuret, Jean-Yves</creatorcontrib><creatorcontrib>Agez, Morgane</creatorcontrib><creatorcontrib>Courbeyrette, Régis</creatorcontrib><creatorcontrib>Amigues, Béatrice</creatorcontrib><creatorcontrib>Becker, Emmanuelle</creatorcontrib><creatorcontrib>Neumann, Jean-Michel</creatorcontrib><creatorcontrib>Guerois, Raphaël</creatorcontrib><creatorcontrib>Mann, Carl</creatorcontrib><creatorcontrib>Ochsenbein, Françoise</creatorcontrib><creatorcontrib>Felsenfeld, Gary</creatorcontrib><title>Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.</description><subject>Animals</subject><subject>Binding Sites</subject><subject>Biochemistry, Molecular Biology</subject><subject>Biological Sciences</subject><subject>Biophysics</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Chemical equilibrium</subject><subject>Chickens</subject><subject>DNA</subject><subject>DNA damage</subject><subject>DNA repair</subject><subject>Genetic mutation</subject><subject>Glutathione Transferase - chemistry</subject><subject>Glutathione Transferase - metabolism</subject><subject>Histones</subject><subject>Histones - chemistry</subject><subject>Histones - metabolism</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Magnetic Resonance Spectroscopy</subject><subject>Models, Molecular</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Nucleosomes</subject><subject>Phenotypes</subject><subject>Plasmids</subject><subject>Protein Conformation</subject><subject>Protein Structure, Secondary</subject><subject>Proteins</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90c1v0zAYBnALgVgZnLkgsDggOGR7_RU7F6QyMVqpEgfghmS5jk1TpXGxnQH_PQ6tVtiBS6wov_dx7AehpwQuCEh2uR9MugABQHhDgN5DMwINqWrewH00A6CyUpzyM_QopS0ANELBQ3RGhOIgqZihr59yHG0eo-nxO5O6hH2IOG8cXg7ZRWNzFwYcPJ4nT_CPLm_woks5DA4vGDZDi5c54etx-ANLyHK37ztrprf0GD3wpk_uyXE9R1-u33--WlSrjx-WV_NVZUVNcmWlqqlqpW-oWDfCCbo2nJmGtdbQlpuaOV_Ltjz5WjHO2rU3tRdQOCdScHaO3h5y9-N651rrhlzOo_ex25n4SwfT6X-_DN1Gfws3moCSDYUS8OYQsLkztpivtHVGA5GccypvSLGvjpvF8H10Ketdl6zrezO4MCZNpJJEgCrw5R24DWMsd5Q0BcLqmlFW0OUB2RhSis7fbk9ATxXrqWJ9qrhMPP_7sCd_7LSAF0cwTZ7iaPk1LRo5idf_F9qPfZ_dz1zoswPdltLjrWVMCsoU-w3-E8Le</recordid><startdate>20050426</startdate><enddate>20050426</enddate><creator>Mousson, Florence</creator><creator>Lautrette, Aurélie</creator><creator>Thuret, Jean-Yves</creator><creator>Agez, Morgane</creator><creator>Courbeyrette, Régis</creator><creator>Amigues, Béatrice</creator><creator>Becker, Emmanuelle</creator><creator>Neumann, Jean-Michel</creator><creator>Guerois, Raphaël</creator><creator>Mann, Carl</creator><creator>Ochsenbein, Françoise</creator><creator>Felsenfeld, Gary</creator><general>National Academy of Sciences</general><general>National Acad Sciences</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>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope><scope>1XC</scope><scope>5PM</scope><orcidid>https://orcid.org/0000-0002-7673-0582</orcidid></search><sort><creationdate>20050426</creationdate><title>Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications</title><author>Mousson, Florence ; Lautrette, Aurélie ; Thuret, Jean-Yves ; Agez, Morgane ; Courbeyrette, Régis ; Amigues, Béatrice ; Becker, Emmanuelle ; Neumann, Jean-Michel ; Guerois, Raphaël ; Mann, Carl ; Ochsenbein, Françoise ; Felsenfeld, Gary</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c561t-c78628d7f925b95e52ba43a93dca2d4a63ef67d3ef4b8343dbfa6f50925417543</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>Animals</topic><topic>Binding Sites</topic><topic>Biochemistry, Molecular Biology</topic><topic>Biological Sciences</topic><topic>Biophysics</topic><topic>Cell Cycle Proteins - chemistry</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Chemical equilibrium</topic><topic>Chickens</topic><topic>DNA</topic><topic>DNA damage</topic><topic>DNA repair</topic><topic>Genetic mutation</topic><topic>Glutathione Transferase - chemistry</topic><topic>Glutathione Transferase - metabolism</topic><topic>Histones</topic><topic>Histones - chemistry</topic><topic>Histones - metabolism</topic><topic>Humans</topic><topic>Life Sciences</topic><topic>Magnetic Resonance Spectroscopy</topic><topic>Models, Molecular</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Nucleosomes</topic><topic>Phenotypes</topic><topic>Plasmids</topic><topic>Protein Conformation</topic><topic>Protein Structure, Secondary</topic><topic>Proteins</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - metabolism</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mousson, Florence</creatorcontrib><creatorcontrib>Lautrette, Aurélie</creatorcontrib><creatorcontrib>Thuret, Jean-Yves</creatorcontrib><creatorcontrib>Agez, Morgane</creatorcontrib><creatorcontrib>Courbeyrette, Régis</creatorcontrib><creatorcontrib>Amigues, Béatrice</creatorcontrib><creatorcontrib>Becker, Emmanuelle</creatorcontrib><creatorcontrib>Neumann, Jean-Michel</creatorcontrib><creatorcontrib>Guerois, Raphaël</creatorcontrib><creatorcontrib>Mann, Carl</creatorcontrib><creatorcontrib>Ochsenbein, Françoise</creatorcontrib><creatorcontrib>Felsenfeld, Gary</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors 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>Genetics Abstracts</collection><collection>Hyper Article en Ligne (HAL)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mousson, Florence</au><au>Lautrette, Aurélie</au><au>Thuret, Jean-Yves</au><au>Agez, Morgane</au><au>Courbeyrette, Régis</au><au>Amigues, Béatrice</au><au>Becker, Emmanuelle</au><au>Neumann, Jean-Michel</au><au>Guerois, Raphaël</au><au>Mann, Carl</au><au>Ochsenbein, Françoise</au><au>Felsenfeld, Gary</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-04-26</date><risdate>2005</risdate><volume>102</volume><issue>17</issue><spage>5975</spage><epage>5980</epage><pages>5975-5980</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Asf1 is a conserved histone chaperone implicated in nucleosome assembly, transcriptional silencing, and the cellular response to DNA damage. We solved the NMR solution structure of the N-terminal functional domain of the human Asf1a isoform, and we identified by NMR chemical shift mapping a surface of Asf1a that binds the C-terminal helix of histone H3. This binding surface forms a highly conserved hydrophobic groove surrounded by charged residues. Mutations within this binding site decreased the affinity of Asf1a for the histone H3/H4 complex in vitro, and the same mutations in the homologous yeast protein led to transcriptional silencing defects, DNA damage sensitivity, and thermosensitive growth. We have thus obtained direct experimental evidence of the mode of binding between a histone and one of its chaperones and genetic data suggesting that this interaction is important in both the DNA damage response and transcriptional silencing.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>15840725</pmid><doi>10.1073/pnas.0500149102</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0002-7673-0582</orcidid><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proceedings of the National Academy of Sciences - PNAS, 2005-04, Vol.102 (17), p.5975-5980 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_pubmed_primary_15840725 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | Animals Binding Sites Biochemistry, Molecular Biology Biological Sciences Biophysics Cell Cycle Proteins - chemistry Cell Cycle Proteins - metabolism Chemical equilibrium Chickens DNA DNA damage DNA repair Genetic mutation Glutathione Transferase - chemistry Glutathione Transferase - metabolism Histones Histones - chemistry Histones - metabolism Humans Life Sciences Magnetic Resonance Spectroscopy Models, Molecular Mutagenesis, Site-Directed Mutation Nucleosomes Phenotypes Plasmids Protein Conformation Protein Structure, Secondary Proteins Recombinant Fusion Proteins - chemistry Recombinant Proteins - chemistry Recombinant Proteins - metabolism Yeast Yeasts |
| title | Structural Basis for the Interaction of Asf1 with Histone H3 and Its Functional Implications |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-15T15%3A50%3A51IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20Basis%20for%20the%20Interaction%20of%20Asf1%20with%20Histone%20H3%20and%20Its%20Functional%20Implications&rft.jtitle=Proceedings%20of%20the%20National%20Academy%20of%20Sciences%20-%20PNAS&rft.au=Mousson,%20Florence&rft.date=2005-04-26&rft.volume=102&rft.issue=17&rft.spage=5975&rft.epage=5980&rft.pages=5975-5980&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.0500149102&rft_dat=%3Cjstor_pubme%3E3375238%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=201366323&rft_id=info:pmid/15840725&rft_jstor_id=3375238&rfr_iscdi=true |