Journal
PLOS GENETICS
Volume 11, Issue 1, Pages -Publisher
PUBLIC LIBRARY SCIENCE
DOI: 10.1371/journal.pgen.1004931
Keywords
-
Categories
Funding
- Wellcome Trust [083524/Z/07/Z]
- ZFF (Zentrale Forschungsforderung, Universitat Kassel, Germany)
- Deutsche Forschungsgemeinschaft Bonn, Germany [SCHA 750/18-1]
- Biotechnology and Biological Sciences Research Council (BBSRC) [BB/F0191629/1, BB/F019106/1]
- FEBS Summer Studentship
- BBSRC [BB/F019629/1, BB/F019106/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/F019106/1, BB/F019629/1] Funding Source: researchfish
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available