Phosphorylation of Elp1 by Hrr25 is required for Elongator-dependent tRNA modification in yeast

Wael Abdel-Fattah, Daniel Jablonowski, Rachael Di Santo, Kathrin L. Thüring, Viktor Scheidt, Alexander Hammermeister, Sara ten Have, Mark Helm, Raffael Schaffrath (Lead / Corresponding author), Michael John Raymond Stark (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    40 Citations (Scopus)


    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.

    Original languageEnglish
    Article numbere1004931
    Number of pages16
    JournalPLoS Genetics
    Issue number1
    Publication statusPublished - 8 Jan 2015

    ASJC Scopus subject areas

    • Genetics
    • Molecular Biology
    • Ecology, Evolution, Behavior and Systematics
    • Cancer Research
    • Genetics(clinical)


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