Datum
2023-08-08Autor
Arend, MeikeÜtkür, KorayHawer, HarmenMayer, KlausRanjan, NamitAdrian, LorenzBrinkmann, UlrichSchaffrath, RaffaelSchlagwort
540 Chemie 570 Biowissenschaften, Biologie 610 Medizin Hefeartige PilzeToxinDiphtherietoxinMetadata
Zur Langanzeige
Aufsatz
Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2
Zusammenfassung
In yeast, Elongator-dependent tRNA modifications are regulated by the Kti11•Kti13 dimer and hijacked for cell killing by zymocin, a tRNase ribotoxin. Kti11 (alias Dph3) also controls modification of elongation factor 2 (EF2) with diphthamide, the target for lethal ADP-ribosylation by diphtheria toxin (DT). Diphthamide formation on EF2 involves four biosynthetic steps encoded by the DPH1-DPH7 network and an ill-defined KTI13 function. On further examining the latter gene in yeast, we found that kti13Δ null-mutants maintain unmodified EF2 able to escape ADP-ribosylation by DT and to survive EF2 inhibition by sordarin, a diphthamide-dependent antifungal.
Consistently, mass spectrometry shows kti13Δ cells are blocked in proper formation of amino-carboxyl-propyl-EF2, the first diphthamide pathway intermediate. Thus, apart from their common function in tRNA modification, both Kti11/Dph3 and Kti13 share roles in the initiation step of EF2 modification. We suggest an alias KTI13/DPH8 nomenclature indicating dual-functionality analogous to KTI11/DPH3.
Consistently, mass spectrometry shows kti13Δ cells are blocked in proper formation of amino-carboxyl-propyl-EF2, the first diphthamide pathway intermediate. Thus, apart from their common function in tRNA modification, both Kti11/Dph3 and Kti13 share roles in the initiation step of EF2 modification. We suggest an alias KTI13/DPH8 nomenclature indicating dual-functionality analogous to KTI11/DPH3.
Zitierform
In: Microbial Cell Volume 10 / Issue No. 9 (2023-08-08) , S. 195 - 203 ; eissn:2311-2638Förderhinweis
Gefördert durch den Publikationsfonds der Universität KasselZitieren
@article{doi:10.17170/kobra-202312019147,
author={Arend, Meike and Ütkür, Koray and Hawer, Harmen and Mayer, Klaus and Ranjan, Namit and Adrian, Lorenz and Brinkmann, Ulrich and Schaffrath, Raffael},
title={Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2},
journal={Microbial Cell},
year={2023}
}
0500 Oax 0501 Text $btxt$2rdacontent 0502 Computermedien $bc$2rdacarrier 1100 2023$n2023 1500 1/eng 2050 ##0##http://hdl.handle.net/123456789/15249 3000 Arend, Meike 3010 Ütkür, Koray 3010 Hawer, Harmen 3010 Mayer, Klaus 3010 Ranjan, Namit 3010 Adrian, Lorenz 3010 Brinkmann, Ulrich 3010 Schaffrath, Raffael 4000 Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2 / Arend, Meike 4030 4060 Online-Ressource 4085 ##0##=u http://nbn-resolving.de/http://hdl.handle.net/123456789/15249=x R 4204 \$dAufsatz 4170 5550 {{Hefeartige Pilze}} 5550 {{Toxin}} 5550 {{Diphtherietoxin}} 7136 ##0##http://hdl.handle.net/123456789/15249
2023-12-01T11:54:37Z 2023-12-01T11:54:37Z 2023-08-08 doi:10.17170/kobra-202312019147 http://hdl.handle.net/123456789/15249 Gefördert durch den Publikationsfonds der Universität Kassel eng Namensnennung 4.0 International http://creativecommons.org/licenses/by/4.0/ budding yeast EF2 diphthamide modification diphtheria toxin tRNA modification elongator tRNase zymocin 540 570 610 Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2 Aufsatz In yeast, Elongator-dependent tRNA modifications are regulated by the Kti11•Kti13 dimer and hijacked for cell killing by zymocin, a tRNase ribotoxin. Kti11 (alias Dph3) also controls modification of elongation factor 2 (EF2) with diphthamide, the target for lethal ADP-ribosylation by diphtheria toxin (DT). Diphthamide formation on EF2 involves four biosynthetic steps encoded by the DPH1-DPH7 network and an ill-defined KTI13 function. On further examining the latter gene in yeast, we found that kti13Δ null-mutants maintain unmodified EF2 able to escape ADP-ribosylation by DT and to survive EF2 inhibition by sordarin, a diphthamide-dependent antifungal. Consistently, mass spectrometry shows kti13Δ cells are blocked in proper formation of amino-carboxyl-propyl-EF2, the first diphthamide pathway intermediate. Thus, apart from their common function in tRNA modification, both Kti11/Dph3 and Kti13 share roles in the initiation step of EF2 modification. We suggest an alias KTI13/DPH8 nomenclature indicating dual-functionality analogous to KTI11/DPH3. open access Arend, Meike Ütkür, Koray Hawer, Harmen Mayer, Klaus Ranjan, Namit Adrian, Lorenz Brinkmann, Ulrich Schaffrath, Raffael doi:10.15698/mic2023.09.804 Hefeartige Pilze Toxin Diphtherietoxin publishedVersion eissn:2311-2638 Issue No. 9 Microbial Cell 195 - 203 Volume 10 false
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