Claim · model-written summary
dph2 mutants have attenuated TOR kinase activity
- Taxon
- Arabidopsis
Arabidopsist0 - Material
- dph2e0
- Gene
- dph2e0
- Outcome
- TARGET OF RAPAMYCIN (TOR) kinase activitye0
- Direction
- attenuatede0
Not reportedCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingValueQualifier
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“increased ribosomal -1 frameshifting error rates and attenuated TARGET OF RAPAMYCIN (TOR) kinase activity in dph2 mutants also phenocopy the dph1 mutant”
t0“Arabidopsis”
Title
Hongliang Zhang; Nadežda Janina; Koray Ütkür; et al. PLANT PHYSIOLOGY 2025. doi:10.1093/plphys/kiaf128
Other claims from this paper (11)
- Observation DPH2 is required for diphthamide biosynthesis
- Observation DPH2 localizes to the cytosol
- Observation DPH2 physically interacts with AtDPH1
- Observation dph2 mutants have shorter primary roots than wild type
- Observation dph2 mutants have smaller rosettes than wild type
- Observation dph2 mutants have increased ribosomal -1 frameshifting error rates
- Observation dph1 and dph2 mutants are hypersensitive to elevated light intensities
- Observation dph1 and dph2 mutants are hypersensitive to oxidative stress
- Observation Wild-type seedlings accumulate diphthamide-unmodified eEF2 under oxidative stress
- Observation Both mutants share deregulation of 1,186 transcripts associated with environmental and hormone responses
- Observation AtDPH1 and AtDPH2 do not complement corresponding yeast mutants