Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2
| dc.date.accessioned | 2023-12-01T11:54:37Z | |
| dc.date.available | 2023-12-01T11:54:37Z | |
| dc.date.issued | 2023-08-08 | |
| dc.identifier | doi:10.17170/kobra-202312019147 | |
| dc.identifier.uri | http://hdl.handle.net/123456789/15249 | |
| dc.description.sponsorship | Gefördert durch den Publikationsfonds der Universität Kassel | |
| dc.language.iso | eng | |
| dc.rights | Namensnennung 4.0 International | * |
| dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
| dc.subject | budding yeast | eng |
| dc.subject | EF2 diphthamide modification | eng |
| dc.subject | diphtheria toxin | eng |
| dc.subject | tRNA modification | eng |
| dc.subject | elongator | eng |
| dc.subject | tRNase zymocin | eng |
| dc.subject.ddc | 540 | |
| dc.subject.ddc | 570 | |
| dc.subject.ddc | 610 | |
| dc.title | Yeast gene KTI13 (alias DPH8) operates in the initiation step of diphthamide synthesis on elongation factor 2 | eng |
| dc.type | Aufsatz | |
| dcterms.abstract | 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. | eng |
| dcterms.accessRights | open access | |
| dcterms.creator | Arend, Meike | |
| dcterms.creator | Ütkür, Koray | |
| dcterms.creator | Hawer, Harmen | |
| dcterms.creator | Mayer, Klaus | |
| dcterms.creator | Ranjan, Namit | |
| dcterms.creator | Adrian, Lorenz | |
| dcterms.creator | Brinkmann, Ulrich | |
| dcterms.creator | Schaffrath, Raffael | |
| dc.relation.doi | doi:10.15698/mic2023.09.804 | |
| dc.subject.swd | Hefeartige Pilze | ger |
| dc.subject.swd | Toxin | ger |
| dc.subject.swd | Diphtherietoxin | ger |
| dc.type.version | publishedVersion | |
| dcterms.source.identifier | eissn:2311-2638 | |
| dcterms.source.issue | Issue No. 9 | |
| dcterms.source.journal | Microbial Cell | eng |
| dcterms.source.pageinfo | 195 - 203 | |
| dcterms.source.volume | Volume 10 | |
| kup.iskup | false |
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