Molecular interaction of replicase protein geminivirus from Pesisir Selatan isolate with Ankyrin-NPR1 domain

Knowing the effect of geminivirus protein Rep interaction with ankyrin domain of the NPR1 [Non-expressor of pathogenesis-related 1] gene was aimed to understand how the suppressing of expression resistance genes associated with the event of a pathogen attack. Interactions that occur will affect the work of the NPR1 protein as a transcription factor. EMSA [Electrophoretic Mobility Shift Assay] technique was applied to study their interaction. The ratio of proteins with nucleic acids was 7.6 ng/μL Rep x 100 ng/μL ankyrin [also in the mutant] and 7.6 ng/μL Rep x 5 ng/μL ankyrin was able to visualize the binding activity. Modeling, simulations, and interaction with NPR1 protein mutations were also carried out to understand the effect of the interactions. Three-dimensional analyses of NPR1 and mutant NPR1 proteins showed different binding positions and interactions. The complex interaction formed between non-mutant NPR1 protein and Rep protein had docking score -542.04 and - 523.56 respectively. The mutant sequence showed no binding.