Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.
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 wor...
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS Genetics |
| Online Access: | https://doi.org/10.1371/journal.pgen.1004931 |
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| author | Wael Abdel-Fattah Daniel Jablonowski Rachael Di Santo Kathrin L Thüring Viktor Scheidt Alexander Hammermeister Sara Ten Have Mark Helm Raffael Schaffrath Michael J R Stark |
| author_facet | Wael Abdel-Fattah Daniel Jablonowski Rachael Di Santo Kathrin L Thüring Viktor Scheidt Alexander Hammermeister Sara Ten Have Mark Helm Raffael Schaffrath Michael J R Stark |
| author_sort | Wael Abdel-Fattah |
| collection | DOAJ |
| description | 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. |
| format | Article |
| id | doaj-art-855b1e29320f4b6fa0c56c51d4d5349f |
| institution | OA Journals |
| issn | 1553-7390 1553-7404 |
| language | English |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Genetics |
| spelling | doaj-art-855b1e29320f4b6fa0c56c51d4d5349f2025-08-20T02:34:09ZengPublic Library of Science (PLoS)PLoS Genetics1553-73901553-74042015-01-01111e100493110.1371/journal.pgen.1004931Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.Wael Abdel-FattahDaniel JablonowskiRachael Di SantoKathrin L ThüringViktor ScheidtAlexander HammermeisterSara Ten HaveMark HelmRaffael SchaffrathMichael J R StarkElongator 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.https://doi.org/10.1371/journal.pgen.1004931 |
| spellingShingle | Wael Abdel-Fattah Daniel Jablonowski Rachael Di Santo Kathrin L Thüring Viktor Scheidt Alexander Hammermeister Sara Ten Have Mark Helm Raffael Schaffrath Michael J R Stark Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. PLoS Genetics |
| title | Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. |
| title_full | Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. |
| title_fullStr | Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. |
| title_full_unstemmed | Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. |
| title_short | Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast. |
| title_sort | phosphorylation of elp1 by hrr25 is required for elongator dependent trna modification in yeast |
| url | https://doi.org/10.1371/journal.pgen.1004931 |
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