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http://purl.uniprot.org/citations/25569479http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25569479http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/25569479http://www.w3.org/2000/01/rdf-schema#comment"Elongator is a conserved protein complex comprising six different polypeptides that has been ascribed a wide range of functions, but which is now known to be required for modification of uridine residues in the wobble position of a subset of tRNAs in yeast, plants, worms and mammals. In previous work, we showed that Elongator's largest subunit (Elp1; also known as Iki3) was phosphorylated and implicated the yeast casein kinase I Hrr25 in Elongator function. Here we report identification of nine in vivo phosphorylation sites within Elp1 and show that four of these, clustered close to the Elp1 C-terminus and adjacent to a region that binds tRNA, are important for Elongator's tRNA modification function. Hrr25 protein kinase directly modifies Elp1 on two sites (Ser-1198 and Ser-1202) and through analyzing non-phosphorylatable (alanine) and acidic, phosphomimic substitutions at Ser-1198, Ser-1202 and Ser-1209, we provide evidence that phosphorylation plays a positive role in the tRNA modification function of Elongator and may regulate the interaction of Elongator both with its accessory protein Kti12 and with Hrr25 kinase."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1004931"xsd:string
http://purl.uniprot.org/citations/25569479http://purl.org/dc/terms/identifier"doi:10.1371/journal.pgen.1004931"xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Helm M."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Helm M."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Stark M.J."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Stark M.J."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Schaffrath R."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Schaffrath R."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Scheidt V."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Scheidt V."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Abdel-Fattah W."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Abdel-Fattah W."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Jablonowski D."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Jablonowski D."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Di Santo R."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Di Santo R."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Hammermeister A."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Hammermeister A."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Ten Have S."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Ten Have S."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Thuering K.L."xsd:string
http://purl.uniprot.org/citations/25569479http://purl.uniprot.org/core/author"Thuering K.L."xsd:string