Phosphorylation of Elp1 by Hrr25 Is Required for Elongator-Dependent tRNA Modification in Yeast
- Publikationstyp:
- Zeitschriftenaufsatz
- Metadaten:
-
- Autoren
- Wael Abdel-Fattah
- Daniel Jablonowski
- Rachael Di Santo
- Kathrin L Thuering
- Viktor Scheidt
- Alexander Hammermeister
- Sara ten Have
- Mark Helm
- Raffael Schaffrath
- Michael JR Stark
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000349314600043&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1371/journal.pgen.1004931
- Externe Identifier
- Clarivate Analytics Document Solution ID: CB0KL
- PubMed Identifier: 25569479
- ISSN
- 1553-7404
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- PLOS GENETICS
- Artikelnummer
- ARTN e1004931
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Titel
- Phosphorylation of Elp1 by Hrr25 Is Required for Elongator-Dependent tRNA Modification in Yeast
- Sub types
- Article
- Ausgabe der Zeitschrift
- 11
Datenquelle: Web of Science (Lite)
- Andere Metadatenquellen:
-
- Autoren
- Wael Abdel-Fattah
- Daniel Jablonowski
- Rachael Di Santo
- Kathrin L Thüring
- Viktor Scheidt
- Alexander Hammermeister
- Sara ten Have
- Mark Helm
- Raffael Schaffrath
- Michael JR Stark
- DOI
- 10.1371/journal.pgen.1004931
- Editoren
- Mick F Tuite
- eISSN
- 1553-7404
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- PLoS Genetics
- Sprache
- en
- Online publication date
- 2015
- Paginierung
- e1004931 - e1004931
- Status
- Published online
- Herausgeber
- Public Library of Science (PLoS)
- Herausgeber URL
- http://dx.doi.org/10.1371/journal.pgen.1004931
- Datum der Datenerfassung
- 2022
- Titel
- Phosphorylation of Elp1 by Hrr25 Is Required for Elongator-Dependent tRNA Modification in Yeast
- Ausgabe der Zeitschrift
- 11
Datenquelle: Crossref
- Abstract
- 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.
- Addresses
- Centre for Gene Regulation & Expression, College of Life Sciences, University of Dundee, Dundee, United Kingdom; Institut für Biologie, FG Mikrobiologie, Universität Kassel, Germany.
- Autoren
- Wael Abdel-Fattah
- Daniel Jablonowski
- Rachael Di Santo
- Kathrin L Thüring
- Viktor Scheidt
- Alexander Hammermeister
- Sara Ten Have
- Mark Helm
- Raffael Schaffrath
- Michael JR Stark
- DOI
- 10.1371/journal.pgen.1004931
- eISSN
- 1553-7404
- Externe Identifier
- PubMed Identifier: 25569479
- PubMed Central ID: PMC4287497
- Funding acknowledgements
- Wellcome Trust:
- Wellcome Trust: 097945
- Biotechnology and Biological Sciences Research Council: BB/F019106/1
- Biotechnology and Biological Sciences Research Council: BB/F0191629/1
- Biotechnology and Biological Sciences Research Council: BB/F019629/1
- Wellcome Trust: 083524/Z/07/Z
- Open access
- true
- ISSN
- 1553-7390
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- PLoS genetics
- Schlüsselwörter
- Saccharomyces cerevisiae
- Multiprotein Complexes
- Casein Kinase I
- Alanine
- Adaptor Proteins, Signal Transducing
- Saccharomyces cerevisiae Proteins
- Peptide Elongation Factors
- RNA, Transfer
- Uridine
- Gene Expression Regulation, Fungal
- Phosphorylation
- Phenotype
- Histone Acetyltransferases
- Sprache
- eng
- Medium
- Electronic-eCollection
- Online publication date
- 2015
- Open access status
- Open Access
- Paginierung
- e1004931
- Datum der Veröffentlichung
- 2015
- Status
- Published
- Publisher licence
- CC BY
- Datum der Datenerfassung
- 2015
- Titel
- Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 11
Files
https://journals.plos.org/plosgenetics/article/file?id=10.1371/journal.pgen.1004931&type=printable https://europepmc.org/articles/PMC4287497?pdf=render
Datenquelle: Europe PubMed Central
- Abstract
- 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.
- Date of acceptance
- 2014
- Autoren
- Wael Abdel-Fattah
- Daniel Jablonowski
- Rachael Di Santo
- Kathrin L Thüring
- Viktor Scheidt
- Alexander Hammermeister
- Sara Ten Have
- Mark Helm
- Raffael Schaffrath
- Michael JR Stark
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/25569479
- DOI
- 10.1371/journal.pgen.1004931
- eISSN
- 1553-7404
- Externe Identifier
- PubMed Central ID: PMC4287497
- Funding acknowledgements
- Wellcome Trust: 097945
- Biotechnology and Biological Sciences Research Council: BB/F019106/1
- Biotechnology and Biological Sciences Research Council: BB/F0191629/1
- Wellcome Trust:
- Biotechnology and Biological Sciences Research Council: BB/F019629/1
- Ausgabe der Veröffentlichung
- 1
- Zeitschrift
- PLoS Genet
- Schlüsselwörter
- Adaptor Proteins, Signal Transducing
- Alanine
- Casein Kinase I
- Gene Expression Regulation, Fungal
- Histone Acetyltransferases
- Multiprotein Complexes
- Peptide Elongation Factors
- Phenotype
- Phosphorylation
- RNA, Transfer
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Uridine
- Sprache
- eng
- Country
- United States
- Paginierung
- e1004931
- PII
- PGENETICS-D-14-02297
- Datum der Veröffentlichung
- 2015
- Status
- Published online
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2015
- Titel
- Phosphorylation of Elp1 by Hrr25 is required for elongator-dependent tRNA modification in yeast.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 11
Datenquelle: PubMed
- Beziehungen:
- Eigentum von