Publication Details

Category Text Publication
Reference Category Journals
DOI 10.1038/s41467-022-31712-7
Licence creative commons licence
Title (Primary) Translational fidelity and growth of Arabidopsis require stress-sensitive diphthamide biosynthesis
Author Zhang, H.; Quintana, J.; Ütkür, K.; Adrian, L.; Hawer, H.; Mayer, K.; Gong, X.; Castanedo, L.; Schulten, A.; Janina, N.; Peters, M.; Wirtz, M.; Brinkmann, U.; Schaffrath, R.; Krämer, U.
Source Titel Nature Communications
Year 2022
Department UBT
Volume 13
Page From art. 4009
Language englisch
Topic T7 Bioeconomy
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Abstract 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 Arabidopsis thaliana and requires AtDPH1. Ribosomal −1 frameshifting-error rates are increased in Arabidopsis dph1 mutants, similar to yeast and mice. Compared to the wild type, shorter roots and smaller rosettes of dph1 mutants result from fewer formed cells. TARGET OF RAPAMYCIN (TOR) kinase activity is attenuated, and autophagy is activated, in 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 growt
Persistent UFZ Identifier https://www.ufz.de/index.php?en=20939&ufzPublicationIdentifier=26421
Zhang, H., Quintana, J., Ütkür, K., Adrian, L., Hawer, H., Mayer, K., Gong, X., Castanedo, L., Schulten, A., Janina, N., Peters, M., Wirtz, M., Brinkmann, U., Schaffrath, R., Krämer, U. (2022):
Translational fidelity and growth of Arabidopsis require stress-sensitive diphthamide biosynthesis
Nat. Commun. 13 , art. 4009 10.1038/s41467-022-31712-7