Translational fidelity and growth of Arabidopsis require stress-sensitive diphthamide biosynthesis

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 and Ute Krämer ()
Additional contact information
Hongliang Zhang: Ruhr University Bochum
Julia Quintana: Ruhr University Bochum
Koray Ütkür: University of Kassel
Lorenz Adrian: Helmholtz Centre for Environmental Research—UFZ
Harmen Hawer: University of Kassel
Klaus Mayer: Roche Innovation Center Munich
Xiaodi Gong: University of Heidelberg
Leonardo Castanedo: Ruhr University Bochum
Anna Schulten: Ruhr University Bochum
Nadežda Janina: Ruhr University Bochum
Marcus Peters: Ruhr University Bochum
Markus Wirtz: University of Heidelberg
Ulrich Brinkmann: Roche Innovation Center Munich
Raffael Schaffrath: University of Kassel
Ute Krämer: Ruhr University Bochum

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: 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 growth.

Date: 2022
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DOI: 10.1038/s41467-022-31712-7

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