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http://purl.uniprot.org/citations/16314571http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314571http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/16314571http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0506350102"xsd:string
http://purl.uniprot.org/citations/16314571http://purl.org/dc/terms/identifier"doi:10.1073/pnas.0506350102"xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Li M."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Guan Z."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Guan Z."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Sage H."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Sage H."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Zhou P."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Zhou P."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Greenleaf A.L."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Greenleaf A.L."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Phatnani H.P."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/author"Phatnani H.P."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/date"2005"xsd:gYear
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/name"Proc. Natl. Acad. Sci. U.S.A."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/pages"17636-17641"xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/pages"17636-17641"xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/title"Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1."xsd:string
http://purl.uniprot.org/citations/16314571http://purl.uniprot.org/core/title"Solution structure of the Set2-Rpb1 interacting domain of human Set2 and its interaction with the hyperphosphorylated C-terminal domain of Rpb1."xsd:string