%0 Journal Article %T Phosphorylation of Elp1 by Hrr25 Is Required for Elongator-Dependent tRNA Modification in Yeast %A Alexander Hammermeister %A Daniel Jablonowski %A Kathrin L. Th¨ıring %A Mark Helm %A Michael J. R. Stark %A Rachael Di Santo %A Raffael Schaffrath %A Sara ten Have %A Viktor Scheidt %A Wael Abdel-Fattah %J - %D 2015 %R 10.1371/journal.pgen.1004931 %X 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 %K Phosphorylation %K Transfer RNA %K Yeast %K Alanine %K Uridine %K Saccharomyces cerevisiae %K Phenotypes %K Co-immunoprecipitation %U https://journals.plos.org/plosgenetics/article?id=10.1371/journal.pgen.1004931