Dataset Information

Characterization of the diphthamide modification of eEF2 in Arabidopsis thaliana

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.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Cell Culture

SUBMITTER: Lorenz Adrian

LAB HEAD: Ute Kraemer

PROVIDER: PXD034873 | Pride | 2022-08-11

REPOSITORIES: Pride

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Publications

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

Zhang Hongliang H Quintana Julia J Ütkür Koray K Adrian Lorenz L Hawer Harmen H Mayer Klaus K Gong Xiaodi X Castanedo Leonardo L Schulten Anna A Janina Nadežda N Peters Marcus M Wirtz Markus M Brinkmann Ulrich U Schaffrath Raffael R Krämer Ute U

Nature communications 20220711 1

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 Arab ...[more]

PMID: 35817801

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			Action	DRS
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	WT_a.raw	Raw
	WT_b.msf	Msf
	WT_b.raw	Raw
	Y22_10.msf	Msf