Solution Structure of the Set2-Rpb1 Interacting Domain of Human Set2 and Its Interaction with the Hyperphosphorylated C-Terminal Domain of Rpb1
The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from y...
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| Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2005-12, Vol.102 (49), p.17636-17641 |
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| container_issue | 49 |
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| container_title | Proceedings of the National Academy of Sciences - PNAS |
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| creator | Li, Ming Hemali P. Phatnani Guan, Ziqiang Harvey Sage Greenleaf, Arno L. Zhou, Pei |
| description | The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD. |
| doi_str_mv | 10.1073/pnas.0506350102 |
| format | Article |
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Phatnani ; Guan, Ziqiang ; Harvey Sage ; Greenleaf, Arno L. ; Zhou, Pei</creator><creatorcontrib>Li, Ming ; Hemali P. Phatnani ; Guan, Ziqiang ; Harvey Sage ; Greenleaf, Arno L. ; Zhou, Pei</creatorcontrib><description>The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0506350102</identifier><identifier>PMID: 16314571</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Amino Acid Sequence ; Amino acids ; Biological Sciences ; Biophysics ; Charge transfer devices ; Enzymes ; Genes ; Histones ; Humans ; Methyltransferases - chemistry ; Methyltransferases - genetics ; Methyltransferases - metabolism ; Models, Molecular ; Molecular Sequence Data ; Mutation - genetics ; Nuclear Magnetic Resonance, Biomolecular ; Nuclear structure ; Peptides ; Phosphates ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Proteins ; Ribonucleic acid ; RNA ; RNA Polymerase II - chemistry ; RNA Polymerase II - metabolism ; Sequence Alignment ; Sequence Homology, Amino Acid ; Social interaction ; Titration ; Yeast ; Yeasts</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2005-12, Vol.102 (49), p.17636-17641</ispartof><rights>Copyright 2005 National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Dec 6, 2005</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-c529t-8fbcfea23355c2db5d1dc9d3879d74102f08bffd43dacdd7f88bc313e5fe77da3</citedby><cites>FETCH-LOGICAL-c529t-8fbcfea23355c2db5d1dc9d3879d74102f08bffd43dacdd7f88bc313e5fe77da3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/102/49.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/4152779$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/4152779$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16314571$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, Ming</creatorcontrib><creatorcontrib>Hemali P. Phatnani</creatorcontrib><creatorcontrib>Guan, Ziqiang</creatorcontrib><creatorcontrib>Harvey Sage</creatorcontrib><creatorcontrib>Greenleaf, Arno L.</creatorcontrib><creatorcontrib>Zhou, Pei</creatorcontrib><title>Solution Structure of the Set2-Rpb1 Interacting Domain of Human Set2 and Its Interaction with the Hyperphosphorylated C-Terminal Domain of Rpb1</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biological Sciences</subject><subject>Biophysics</subject><subject>Charge transfer devices</subject><subject>Enzymes</subject><subject>Genes</subject><subject>Histones</subject><subject>Humans</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - genetics</subject><subject>Methyltransferases - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Mutation - genetics</subject><subject>Nuclear Magnetic Resonance, Biomolecular</subject><subject>Nuclear structure</subject><subject>Peptides</subject><subject>Phosphates</subject><subject>Phosphorylation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Ribonucleic acid</subject><subject>RNA</subject><subject>RNA Polymerase II - chemistry</subject><subject>RNA Polymerase II - metabolism</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>Social interaction</subject><subject>Titration</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>eNqF0U1v0zAYB_AIgVgZnLkgFHFA4pDtsR3H8WUSKi-tNAmJjrPl-GVNldjBdoB-Cr4yyVqtgwsHywf_nr_9-MmylwguEDByOTgZL4BCRSggwI-yBQKOiqrk8DhbAGBW1CUuz7JnMe4AgNManmZnqCKopAwtst8b342p9S7fpDCqNAaTe5unrck3JuHi69CgfO2SCVKl1t3mH3wvWzeb1dhLd6dy6XS-TvEEp7yfbdre5az2gwnD1sdphX0nk9H5srgxoW-d7B4Eznc9z55Y2UXz4rifZ98-fbxZrorrL5_Xy_fXhaKYp6K2jbJGYkIoVVg3VCOtuCY145qV009YqBtrdUm0VFozW9eNIogYag1jWpLz7OqQO4xNb7QyLgXZiSG0vQx74WUr_j5x7Vbc-h8CEag5wBTw9hgQ_PfRxCT6NirTddIZP0aBOANaljN88w_c-TFMnUeBARGOcVVP6PKAVPAxBmPvX4JAzJMW86TFadJTxeuHDZz8cbQTeHcEc-UpDouSC8QqUgk7dl0yv9Jk8__Yibw6kF1MPtybElHMGCd_AB46yYI</recordid><startdate>20051206</startdate><enddate>20051206</enddate><creator>Li, Ming</creator><creator>Hemali P. 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Phatnani</au><au>Guan, Ziqiang</au><au>Harvey Sage</au><au>Greenleaf, Arno L.</au><au>Zhou, Pei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Solution Structure of the Set2-Rpb1 Interacting Domain of Human Set2 and Its Interaction with the Hyperphosphorylated C-Terminal Domain of Rpb1</atitle><jtitle>Proceedings of the National Academy of Sciences - PNAS</jtitle><addtitle>Proc Natl Acad Sci U S A</addtitle><date>2005-12-06</date><risdate>2005</risdate><volume>102</volume><issue>49</issue><spage>17636</spage><epage>17641</epage><pages>17636-17641</pages><issn>0027-8424</issn><eissn>1091-6490</eissn><abstract>The phosphorylation state of the C-terminal repeat domain (CTD) of the largest subunit of RNA polymerase II changes as polymerase transcribes a gene, and the distinct forms of the phospho-CTD (PCTD) recruit different nuclear factors to elongating polymerase. The Set2 histone methyltransferase from yeast was recently shown to bind the PCTD of elongating RNA polymerase II by means of a novel domain termed the Set2-Rpb1 interacting (SRI) domain. Here, we report the solution structure of the SRI domain in human Set2 (hSRI domain), which adopts a left-turned three-helix bundle distinctly different from other structurally characterized PCTD-interacting domains. NMR titration experiments mapped the binding surface of the hSRI domain to helices 1 and 2, and Biacore binding studies showed that the domain binds preferably to [Ser-2 + Ser-5]-phosphorylated CTD peptides containing two or more heptad repeats. Point-mutagenesis studies identified five residues critical for PCTD binding. In view of the differential effects of these point mutations on binding to different CTD phosphopeptides, we propose a model for the hSRI domain interaction with the PCTD.</abstract><cop>United States</cop><pub>National Academy of Sciences</pub><pmid>16314571</pmid><doi>10.1073/pnas.0506350102</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino acids Biological Sciences Biophysics Charge transfer devices Enzymes Genes Histones Humans Methyltransferases - chemistry Methyltransferases - genetics Methyltransferases - metabolism Models, Molecular Molecular Sequence Data Mutation - genetics Nuclear Magnetic Resonance, Biomolecular Nuclear structure Peptides Phosphates Phosphorylation Protein Binding Protein Structure, Tertiary Proteins Ribonucleic acid RNA RNA Polymerase II - chemistry RNA Polymerase II - metabolism Sequence Alignment Sequence Homology, Amino Acid Social interaction Titration Yeast Yeasts |
| title | Solution Structure of the Set2-Rpb1 Interacting Domain of Human Set2 and Its Interaction with the Hyperphosphorylated C-Terminal Domain of Rpb1 |
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