Hongliang Zhang, Julia Quintana, Koray Ütkür, Lorenz Adrian, Harmen Hawer, Klaus Mayer, Xiaodi Gong, Leonardo Castanedo, Anna Schulten, Nadežda Janina, Marcus Peters, Markus Wirtz, Ulrich Brinkmann, Raffael Schaffrath, Ute Krämer
- Diphthamide, a post-translationally modified histidine residue of eukaryotic TRANSLATION ELONGATION FACTOR2 (eEF2), is the human host cell-sensitizing target of diphtheria toxin. Diphthamide biosynthesis depends on the 4Fe-4S-cluster protein Dph1 catalyzing the first committed step, as well as Dph2 to Dph7, in yeast and mammals. Here we show that diphthamide modification of eEF2 is conserved in \(\textit {Arabidopsis thaliana}\) and requires AtDPH1. Ribosomal −1 frameshifting-error rates are increased in Arabidopsis \(\it dph1\) mutants, similar to yeast and mice. Compared to the wild type, shorter roots and smaller rosettes of \(\it dph1\) mutants result from fewer formed cells. TARGET OF RAPAMYCIN (TOR) kinase activity is attenuated, and autophagy is activated, in \(\it dph1\) mutants. Under abiotic stress diphthamide-unmodified eEF2 accumulates in wild-type seedlings, most strongly upon heavy metal excess, which is conserved in human cells. In summary, our results suggest that diphthamide contributes to the functionality of the translational machinery monitored by plants to regulate growth.
MetadatenAuthor: | Hongliang ZhangORCiDGND, Julia QuintanaORCiDGND, Koray ÜtkürGND, Lorenz AdrianORCiDGND, Harmen HawerGND, Klaus MayerGND, Xiaodi GongORCiDGND, Leonardo CastanedoORCiDGND, Anna SchultenORCiDGND, Nadežda JaninaORCiDGND, Marcus PetersORCiDGND, Markus WirtzORCiDGND, Ulrich BrinkmannORCiDGND, Raffael SchaffrathORCiDGND, Ute KrämerORCiDGND |
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URN: | urn:nbn:de:hbz:294-104070 |
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DOI: | https://doi.org/10.1038/s41467-022-31712-7 |
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Parent Title (English): | Nature communications |
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Publisher: | Nature Publishing Group UK |
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Place of publication: | London, Vereinigtes Königreich |
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Document Type: | Article |
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Language: | English |
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Date of Publication (online): | 2023/11/16 |
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Date of first Publication: | 2022/07/11 |
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Publishing Institution: | Ruhr-Universität Bochum, Universitätsbibliothek |
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Tag: | Open Access Fonds |
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Volume: | 13 |
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Issue: | Article 4009 |
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First Page: | 4009-1 |
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Last Page: | 4009-14 |
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Note: | Article Processing Charge funded by the Deutsche Forschungsgemeinschaft (DFG) and the Open Access Publication Fund of Ruhr-Universität Bochum. |
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Institutes/Facilities: | Lehrstuhl für Molekulargenetik und Physiologie der Pflanzen |
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Dewey Decimal Classification: | Naturwissenschaften und Mathematik / Biowissenschaften, Biologie, Biochemie |
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open_access (DINI-Set): | open_access |
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faculties: | Fakultät für Biologie und Biotechnologie |
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Licence (English): | Creative Commons - CC BY 4.0 - Attribution 4.0 International |
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