| Autor: |
Meike Arend, Koray Ütkür, Harmen Hawer, Klaus Mayer, Namit Ranjan, Lorenz Adrian, Ulrich Brinkmann, Raffael Schaffrath |
| Jazyk: |
angličtina |
| Rok vydání: |
2022 |
| Předmět: |
|
| Zdroj: |
Microbial Cell, Vol 10, Iss 9, Pp 195-203 (2022) |
| Druh dokumentu: |
article |
| ISSN: |
2311-2638 |
| DOI: |
10.15698/mic2023.09.804 |
| Popis: |
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. |
| Databáze: |
Directory of Open Access Journals |
| Externí odkaz: |
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