Claim · model-written summary
cAPX was S-nitrosylated at the onset of both cell deaths.
- Taxon
- Tobacco
Nicotiana tabacumt0
- Gene
- cytosolic ascorbate peroxidase (cAPX)e0
- Outcome
- S-nitrosylatede0
- Qualifier
- at the onset of both PCDse0
Not reportedMaterialCompoundOrgan / stageInteractorInteractor roleSecond interactorSecond interactor roleTreatmentComparatorSettingDirectionValue
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
t0“Tobacco Bright Yellow-2 Cells”
e0“cytosolic ascorbate peroxidase (cAPX), a key enzyme controlling H2O2 levels in plants, was found to be S-nitrosylated at the onset of both PCDs”
Title
M. C. de Pinto; V. Locato; A. Sgobba; et al. PLANT PHYSIOLOGY 2013. doi:10.1104/pp.113.222703
Other claims from this paper (7)
- Intervention effect Both heat shock and peroxide induced increased S-nitrosylating agents during programmed cell death.
- Intervention effect NO increased during both induced cell deaths, less under peroxide than heat shock.
- Intervention effect GSNO increased in peroxide-treated cells.
- Intervention effect GSNO decreased after heat shock.
- Observation GSNO reductase activity and expression were low after peroxide and high after heat shock.
- Intervention effect Both stimuli induced S-nitrosylated proteins.
- Mechanism S-nitrosylation of cAPX caused a rapid decrease in its activity.