The SAH7 Homologue of the Allergen Ole e 1 Interacts with the Putative Stress Sensor SBP1 (Selenium-Binding Protein 1) in Arabidopsis thaliana .
Chrysanthi ValassakisOrfeas PetropoulosAdamantia AgalouVarvara PodiaNikolaos PapandreouVassiliki A IconomidouKosmas HaralampidisAndreas RoussisPublished in: International journal of molecular sciences (2023)
In this study, we focused on a member of the Ole e 1 domain-containing family, At SAH7, in Arabidopsis thaliana . Our lab reports for the first time on this protein, At SAH7, that was found to interact with Selenium-binding protein 1 ( At SBP1). We studied by GUS assisted promoter deletion analysis the expression pattern of AtSAH7 and determined that the sequence 1420 bp upstream of the transcription start can act as a minimal promoter inducing expression in vasculature tissues. Moreover, mRNA levels of AtSAH7 were acutely increased under selenite treatment in response to oxidative stress. We confirmed the aforementioned interaction in vivo, in silico and in planta. Following a bimolecular fluorescent complementation approach, we determined that the subcellular localization of the At SAH7 and the AtSAH7 / At SBP1 interaction occur in the ER. Our results indicate the participation of At SAH7 in a biochemical network regulated by selenite, possibly associated with responses to ROS production.
Keyphrases
- binding protein
- arabidopsis thaliana
- oxidative stress
- gene expression
- transcription factor
- dna methylation
- dna damage
- poor prognosis
- physical activity
- cell death
- quantum dots
- living cells
- adverse drug
- reactive oxygen species
- combination therapy
- heat stress
- induced apoptosis
- amino acid
- label free
- heat shock
- protein protein