Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator
- Publication type:
- Journal article
- Metadata:
-
- Autoren
- Roscislaw Krutyholowa
- Alexander Hammermeister
- Rene Zabel
- Wael Abdel-Fattah
- Annekathrin Reinhardt-Tews
- Mark Helm
- Michael JR Stark
- Karin D Breunig
- Raffael Schaffrath
- Sebastian Glatt
- Autoren-URL
- https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=fis-test-1&SrcAuth=WosAPI&KeyUT=WOS:000473756300039&DestLinkType=FullRecord&DestApp=WOS_CPL
- DOI
- 10.1093/nar/gkz190
- eISSN
- 1362-4962
- Externe Identifier
- Clarivate Analytics Document Solution ID: IG4EG
- PubMed Identifier: 30916349
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- NUCLEIC ACIDS RESEARCH
- Paginierung
- 4814 - 4830
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Titel
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator
- Sub types
- Article
- Ausgabe der Zeitschrift
- 47
Data source: Web of Science (Lite)
- Other metadata sources:
-
- Autoren
- Rościsław Krutyhołowa
- Alexander Hammermeister
- Rene Zabel
- Wael Abdel-Fattah
- Annekathrin Reinhardt-Tews
- Mark Helm
- Michael JR Stark
- Karin D Breunig
- Raffael Schaffrath
- Sebastian Glatt
- DOI
- 10.1093/nar/gkz190
- eISSN
- 1362-4962
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Nucleic Acids Research
- Sprache
- en
- Online publication date
- 2019
- Paginierung
- 4814 - 4830
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Herausgeber
- Oxford University Press (OUP)
- Herausgeber URL
- http://dx.doi.org/10.1093/nar/gkz190
- Datum der Datenerfassung
- 2022
- Titel
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator
- Ausgabe der Zeitschrift
- 47
Data source: Crossref
- Abstract
- Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12's nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar mechanisms of tRNA binding and show tRNASec-dependent ATPase activity. In addition, we demonstrate that Kti12 binds directly to Elongator and that ATP hydrolysis is crucial for Elongator to maintain proper tRNA anticodon modification levels in vivo. In summary, our data reveal a hitherto uncharacterized link between two translational control pathways that regulate selenocysteine incorporation and affect ribosomal tRNA selection via specific tRNA modifications.
- Addresses
- Max Planck Research Group at the Malopolska Centre of Biotechnology, Jagiellonian University, Krakow, Poland.
- Autoren
- Rościsław Krutyhołowa
- Alexander Hammermeister
- Rene Zabel
- Wael Abdel-Fattah
- Annekathrin Reinhardt-Tews
- Mark Helm
- Michael JR Stark
- Karin D Breunig
- Raffael Schaffrath
- Sebastian Glatt
- DOI
- 10.1093/nar/gkz190
- eISSN
- 1362-4962
- Externe Identifier
- PubMed Identifier: 30916349
- PubMed Central ID: PMC6511879
- Funding acknowledgements
- National Science Centre: UMO-2015/19/B/NZ1/00343
- Biotechnology and Biological Sciences Research Council: BB/F019106/1
- Biotechnology and Biological Sciences Research Council: BB/F0191629/1
- Open access
- true
- ISSN
- 0305-1048
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Nucleic acids research
- Schlüsselwörter
- Ribosomes
- Saccharomyces cerevisiae
- Chaetomium
- Adaptor Proteins, Signal Transducing
- Carrier Proteins
- Saccharomyces cerevisiae Proteins
- RNA, Transfer
- Anticodon
- Uridine
- Crystallography, X-Ray
- RNA Processing, Post-Transcriptional
- Protein Conformation
- Adenosine Triphosphatases
- Sprache
- eng
- Medium
- Open access status
- Open Access
- Paginierung
- 4814 - 4830
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Publisher licence
- CC BY-NC
- Datum der Datenerfassung
- 2019
- Titel
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.
- Sub types
- Research Support, Non-U.S. Gov't
- research-article
- Journal Article
- Ausgabe der Zeitschrift
- 47
Files
https://europepmc.org/articles/PMC6511879?pdf=render
Data source: Europe PubMed Central
- Abstract
- Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12's nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar mechanisms of tRNA binding and show tRNASec-dependent ATPase activity. In addition, we demonstrate that Kti12 binds directly to Elongator and that ATP hydrolysis is crucial for Elongator to maintain proper tRNA anticodon modification levels in vivo. In summary, our data reveal a hitherto uncharacterized link between two translational control pathways that regulate selenocysteine incorporation and affect ribosomal tRNA selection via specific tRNA modifications.
- Date of acceptance
- 2019
- Autoren
- Rościsław Krutyhołowa
- Alexander Hammermeister
- Rene Zabel
- Wael Abdel-Fattah
- Annekathrin Reinhardt-Tews
- Mark Helm
- Michael JR Stark
- Karin D Breunig
- Raffael Schaffrath
- Sebastian Glatt
- Autoren-URL
- https://www.ncbi.nlm.nih.gov/pubmed/30916349
- DOI
- 10.1093/nar/gkz190
- eISSN
- 1362-4962
- Externe Identifier
- PubMed Central ID: PMC6511879
- Funding acknowledgements
- Biotechnology and Biological Sciences Research Council: BB/F019106/1
- Ausgabe der Veröffentlichung
- 9
- Zeitschrift
- Nucleic Acids Res
- Schlüsselwörter
- Adaptor Proteins, Signal Transducing
- Adenosine Triphosphatases
- Anticodon
- Carrier Proteins
- Chaetomium
- Crystallography, X-Ray
- Protein Conformation
- RNA Processing, Post-Transcriptional
- RNA, Transfer
- Ribosomes
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Uridine
- Sprache
- eng
- Country
- England
- Paginierung
- 4814 - 4830
- PII
- 5420542
- Datum der Veröffentlichung
- 2019
- Status
- Published
- Datum, an dem der Datensatz öffentlich gemacht wurde
- 2019
- Titel
- Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator.
- Sub types
- Journal Article
- Research Support, Non-U.S. Gov't
- Ausgabe der Zeitschrift
- 47
Data source: PubMed
- Beziehungen:
- Property of