Journal
PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS
Volume 85, Issue 10, Pages 1891-1901Publisher
WILEY
DOI: 10.1002/prot.25343
Keywords
abscisic acid (ABA); allergen; dimerization; Fra a 1-Associated Protein (FaAP); plant defense; protein-protein interaction; PR-10 protein family; strawberry allergen Fra a 1.01E/1.02/1.03; time resolved DNA-switching measurements; yeast two-hybrid
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The strawberry fruit allergens Fra a 1.01E, Fra a 1.02 and Fra a 1.03 belong to the group of pathogenesis-related 10 (PR-10) proteins and are homologs of the major birch pollen Bet v 1 and apple allergen Mal d 1. Bet v 1 related proteins are the most extensively studied allergens but their physiological function in planta remains elusive. Since Mal d 1-Associated Protein has been previously identified as interaction partner of Mal d 1 we studied the binding of the orthologous Fra a 1-Associated Protein (FaAP) to Fra a 1.01E/1.02/1.03. As the C-terminal sequence of FaAP showed strong auto-activation activity in yeast 2-hybrid analysis a novel time resolved DNA-switching system was successfully applied. Fra a 1.01E, Fra a 1.02, and Fra a 1.03 bind to FaAP with KD of 4.561.1, 1563, and 1162 nM, respectively. Fra a 1.01E forms a dimer, whereas Fra a 1.02 and Fra a 1.03 bind as monomer. The results imply that PR-10 proteins might be integrated into a protein-interaction network and FaAP binding appears to be essential for the physiological function of the Fra a 1 proteins.
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