Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D
Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles...
Gespeichert in:
| Veröffentlicht in: | Proc. Natl. Acad. Sci. USA 2014-06, Vol.111 (25), p.9103-9108 |
|---|---|
| Hauptverfasser: | , , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 9108 |
|---|---|
| container_issue | 25 |
| container_start_page | 9103 |
| container_title | Proc. Natl. Acad. Sci. USA |
| container_volume | 111 |
| creator | Bhattacharya, Suparna Lou, Xiaohua Hwang, Peter Rajashankar, Kanagalaghatta R. Wang, Xiaoping Gustafsson, Jan-Åke Fletterick, Robert J. Jacobson, Raymond H. Webb, Paul |
| description | Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1–TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1–TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks. |
| doi_str_mv | 10.1073/pnas.1408293111 |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_proqu</sourceid><recordid>TN_cdi_proquest_miscellaneous_1832257109</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>23802488</jstor_id><sourcerecordid>23802488</sourcerecordid><originalsourceid>FETCH-LOGICAL-c584t-f22510852774c7d03d6cbb40863dc8792c5dafe0af76bdc7d882e10ccc84841c3</originalsourceid><addsrcrecordid>eNqNksFuEzEQhi0EoiVw5gSs4MKBtDO2d9d7QaoKhUiVOLQ9IsvxehNHGzvYXgQ33oE35EnwNiEBLnAaWf7m93j-n5DHCCcINTvdOBVPkIOgDUPEO-QYocFpxRu4S44BaD0VnPIj8iDGFQA0pYD75IjyhtYlbY7Jx6sUBp2GoPpCubboBqeT9S4frYt2sUy5Jl9cn13gj2_fc6lfFaqIw1z79aY3XwrfFSkoF3Wwm7Gz6JROPhSzWfHmIbnXqT6aR7s6ITcXb6_P308vP7ybnZ9dTnUpeJp2lJYIoqR1zXXdAmsrPZ_nX1Ws1aJuqC5b1RlQXV3N20wIQQ2C1lpwwVGzCXm91d0M87VptXF5pF5ugl2r8FV6ZeWfN84u5cJ_lhxqISqeBZ5vBXxMVkZtk9FL7Z0zOknMC6YMMvRy90rwnwYTk1zbqE3fK2f8ECUKlj9SZwf-AwU2mkHx32iZh0SGt-iLv9CVH0L26pZipWDjoBNyuqV08DEG0-33gCDH1MgxNfKQmtzx9Pf17flfMcnAsx0wdu7lECUtZYPAMvFkS6xiNv-gwARQLsRBoVNeqkWwUd5cUcAKADlnjLKfwIXZjA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1543583402</pqid></control><display><type>article</type><title>Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D</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>Bhattacharya, Suparna ; Lou, Xiaohua ; Hwang, Peter ; Rajashankar, Kanagalaghatta R. ; Wang, Xiaoping ; Gustafsson, Jan-Åke ; Fletterick, Robert J. ; Jacobson, Raymond H. ; Webb, Paul</creator><creatorcontrib>Bhattacharya, Suparna ; Lou, Xiaohua ; Hwang, Peter ; Rajashankar, Kanagalaghatta R. ; Wang, Xiaoping ; Gustafsson, Jan-Åke ; Fletterick, Robert J. ; Jacobson, Raymond H. ; Webb, Paul ; Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><description>Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1–TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1–TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.1408293111</identifier><identifier>PMID: 24927529</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>acetyltransferases ; Binding Sites ; Biological Sciences ; Cell lines ; Chromatin ; Cradles ; DNA-directed RNA polymerase ; Epigenetics ; Eukaryotes ; Genes ; Histone Acetyltransferases - chemistry ; Histones ; Histones - chemistry ; Humans ; hydrophobicity ; multiprotein complexes ; Multiprotein Complexes - chemistry ; Phosphorylation ; Protein Binding ; Protein Structure, Quaternary ; Proteins ; RNA ; serine ; TATA-Binding Protein Associated Factors - chemistry ; transcription (genetics) ; Transcription Factor TFIID - chemistry ; Transcription factors ; Yeast ; Yeasts</subject><ispartof>Proc. Natl. Acad. Sci. USA, 2014-06, Vol.111 (25), p.9103-9108</ispartof><rights>copyright © 1993—2008 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 24, 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c584t-f22510852774c7d03d6cbb40863dc8792c5dafe0af76bdc7d882e10ccc84841c3</citedby><cites>FETCH-LOGICAL-c584t-f22510852774c7d03d6cbb40863dc8792c5dafe0af76bdc7d882e10ccc84841c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/111/25.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23802488$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23802488$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27903,27904,53769,53771,57995,58228</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24927529$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/1140230$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Bhattacharya, Suparna</creatorcontrib><creatorcontrib>Lou, Xiaohua</creatorcontrib><creatorcontrib>Hwang, Peter</creatorcontrib><creatorcontrib>Rajashankar, Kanagalaghatta R.</creatorcontrib><creatorcontrib>Wang, Xiaoping</creatorcontrib><creatorcontrib>Gustafsson, Jan-Åke</creatorcontrib><creatorcontrib>Fletterick, Robert J.</creatorcontrib><creatorcontrib>Jacobson, Raymond H.</creatorcontrib><creatorcontrib>Webb, Paul</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D</title><title>Proc. Natl. Acad. Sci. USA</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1–TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1–TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.</description><subject>acetyltransferases</subject><subject>Binding Sites</subject><subject>Biological Sciences</subject><subject>Cell lines</subject><subject>Chromatin</subject><subject>Cradles</subject><subject>DNA-directed RNA polymerase</subject><subject>Epigenetics</subject><subject>Eukaryotes</subject><subject>Genes</subject><subject>Histone Acetyltransferases - chemistry</subject><subject>Histones</subject><subject>Histones - chemistry</subject><subject>Humans</subject><subject>hydrophobicity</subject><subject>multiprotein complexes</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Structure, Quaternary</subject><subject>Proteins</subject><subject>RNA</subject><subject>serine</subject><subject>TATA-Binding Protein Associated Factors - chemistry</subject><subject>transcription (genetics)</subject><subject>Transcription Factor TFIID - chemistry</subject><subject>Transcription factors</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNksFuEzEQhi0EoiVw5gSs4MKBtDO2d9d7QaoKhUiVOLQ9IsvxehNHGzvYXgQ33oE35EnwNiEBLnAaWf7m93j-n5DHCCcINTvdOBVPkIOgDUPEO-QYocFpxRu4S44BaD0VnPIj8iDGFQA0pYD75IjyhtYlbY7Jx6sUBp2GoPpCubboBqeT9S4frYt2sUy5Jl9cn13gj2_fc6lfFaqIw1z79aY3XwrfFSkoF3Wwm7Gz6JROPhSzWfHmIbnXqT6aR7s6ITcXb6_P308vP7ybnZ9dTnUpeJp2lJYIoqR1zXXdAmsrPZ_nX1Ws1aJuqC5b1RlQXV3N20wIQQ2C1lpwwVGzCXm91d0M87VptXF5pF5ugl2r8FV6ZeWfN84u5cJ_lhxqISqeBZ5vBXxMVkZtk9FL7Z0zOknMC6YMMvRy90rwnwYTk1zbqE3fK2f8ECUKlj9SZwf-AwU2mkHx32iZh0SGt-iLv9CVH0L26pZipWDjoBNyuqV08DEG0-33gCDH1MgxNfKQmtzx9Pf17flfMcnAsx0wdu7lECUtZYPAMvFkS6xiNv-gwARQLsRBoVNeqkWwUd5cUcAKADlnjLKfwIXZjA</recordid><startdate>20140624</startdate><enddate>20140624</enddate><creator>Bhattacharya, Suparna</creator><creator>Lou, Xiaohua</creator><creator>Hwang, Peter</creator><creator>Rajashankar, Kanagalaghatta R.</creator><creator>Wang, Xiaoping</creator><creator>Gustafsson, Jan-Åke</creator><creator>Fletterick, Robert J.</creator><creator>Jacobson, Raymond H.</creator><creator>Webb, Paul</creator><general>National Academy of Sciences</general><general>National Acad Sciences</general><scope>FBQ</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>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>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>7QO</scope><scope>7ST</scope><scope>SOI</scope><scope>OTOTI</scope><scope>5PM</scope></search><sort><creationdate>20140624</creationdate><title>Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D</title><author>Bhattacharya, Suparna ; Lou, Xiaohua ; Hwang, Peter ; Rajashankar, Kanagalaghatta R. ; Wang, Xiaoping ; Gustafsson, Jan-Åke ; Fletterick, Robert J. ; Jacobson, Raymond H. ; Webb, Paul</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c584t-f22510852774c7d03d6cbb40863dc8792c5dafe0af76bdc7d882e10ccc84841c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>acetyltransferases</topic><topic>Binding Sites</topic><topic>Biological Sciences</topic><topic>Cell lines</topic><topic>Chromatin</topic><topic>Cradles</topic><topic>DNA-directed RNA polymerase</topic><topic>Epigenetics</topic><topic>Eukaryotes</topic><topic>Genes</topic><topic>Histone Acetyltransferases - chemistry</topic><topic>Histones</topic><topic>Histones - chemistry</topic><topic>Humans</topic><topic>hydrophobicity</topic><topic>multiprotein complexes</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Structure, Quaternary</topic><topic>Proteins</topic><topic>RNA</topic><topic>serine</topic><topic>TATA-Binding Protein Associated Factors - chemistry</topic><topic>transcription (genetics)</topic><topic>Transcription Factor TFIID - chemistry</topic><topic>Transcription factors</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bhattacharya, Suparna</creatorcontrib><creatorcontrib>Lou, Xiaohua</creatorcontrib><creatorcontrib>Hwang, Peter</creatorcontrib><creatorcontrib>Rajashankar, Kanagalaghatta R.</creatorcontrib><creatorcontrib>Wang, Xiaoping</creatorcontrib><creatorcontrib>Gustafsson, Jan-Åke</creatorcontrib><creatorcontrib>Fletterick, Robert J.</creatorcontrib><creatorcontrib>Jacobson, Raymond H.</creatorcontrib><creatorcontrib>Webb, Paul</creatorcontrib><creatorcontrib>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><collection>AGRIS</collection><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>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>Biotechnology Research Abstracts</collection><collection>Environment Abstracts</collection><collection>Environment Abstracts</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Proc. Natl. Acad. Sci. USA</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bhattacharya, Suparna</au><au>Lou, Xiaohua</au><au>Hwang, Peter</au><au>Rajashankar, Kanagalaghatta R.</au><au>Wang, Xiaoping</au><au>Gustafsson, Jan-Åke</au><au>Fletterick, Robert J.</au><au>Jacobson, Raymond H.</au><au>Webb, Paul</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D</atitle><jtitle>Proc. Natl. Acad. Sci. USA</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2014-06-24</date><risdate>2014</risdate><volume>111</volume><issue>25</issue><spage>9103</spage><epage>9108</epage><pages>9103-9108</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>Transcription factor II D (TFIID) is a multiprotein complex that nucleates formation of the basal transcription machinery. TATA binding protein-associated factors 1 and 7 (TAF1 and TAF7), two subunits of TFIID, are integral to the regulation of eukaryotic transcription initiation and play key roles in preinitiation complex (PIC) assembly. Current models suggest that TAF7 acts as a dissociable inhibitor of TAF1 histone acetyltransferase activity and that this event ensures appropriate assembly of the RNA polymerase II-mediated PIC before transcriptional initiation. Here, we report the 3D structure of a complex of yeast TAF1 with TAF7 at 2.9 Å resolution. The structure displays novel architecture and is characterized by a large predominantly hydrophobic heterodimer interface and extensive cofolding of TAF subunits. There are no obvious similarities between TAF1 and known histone acetyltransferases. Instead, the surface of the TAF1–TAF7 complex contains two prominent conserved surface pockets, one of which binds selectively to an inhibitory trimethylated histone H3 mark on Lys27 in a manner that is also regulated by phosphorylation at the neighboring H3 serine. Our findings could point toward novel roles for the TAF1–TAF7 complex in regulation of PIC assembly via reading epigenetic histone marks.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>24927529</pmid><doi>10.1073/pnas.1408293111</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0027-8424 |
| ispartof | Proc. Natl. Acad. Sci. USA, 2014-06, Vol.111 (25), p.9103-9108 |
| issn | 0027-8424 1091-6490 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1832257109 |
| source | Jstor Complete Legacy; MEDLINE; PubMed Central; Alma/SFX Local Collection; Free Full-Text Journals in Chemistry |
| subjects | acetyltransferases Binding Sites Biological Sciences Cell lines Chromatin Cradles DNA-directed RNA polymerase Epigenetics Eukaryotes Genes Histone Acetyltransferases - chemistry Histones Histones - chemistry Humans hydrophobicity multiprotein complexes Multiprotein Complexes - chemistry Phosphorylation Protein Binding Protein Structure, Quaternary Proteins RNA serine TATA-Binding Protein Associated Factors - chemistry transcription (genetics) Transcription Factor TFIID - chemistry Transcription factors Yeast Yeasts |
| title | Structural and functional insight into TAF1–TAF7, a subcomplex of transcription factor II D |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-27T00%3A51%3A41IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Structural%20and%20functional%20insight%20into%20TAF1%E2%80%93TAF7,%20a%20subcomplex%20of%20transcription%20factor%20II%20D&rft.jtitle=Proc.%20Natl.%20Acad.%20Sci.%20USA&rft.au=Bhattacharya,%20Suparna&rft.aucorp=Argonne%20National%20Lab.%20(ANL),%20Argonne,%20IL%20(United%20States).%20Advanced%20Photon%20Source%20(APS)&rft.date=2014-06-24&rft.volume=111&rft.issue=25&rft.spage=9103&rft.epage=9108&rft.pages=9103-9108&rft.issn=0027-8424&rft.eissn=1091-6490&rft_id=info:doi/10.1073/pnas.1408293111&rft_dat=%3Cjstor_proqu%3E23802488%3C/jstor_proqu%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1543583402&rft_id=info:pmid/24927529&rft_jstor_id=23802488&rfr_iscdi=true |