LOV2-linker-kinase phosphorylates LOV1-containing N-terminal polypeptide substrate via photoreaction of LOV2 in Arabidopsis phototropin1

AbstractPhototropin is a blue light receptor in plants and is thought to be a light-regulated protein kinase. Previously, we defined the role of the photoreceptive domains, LOV1 and 2, in the light activation of the kinase in Arabidopsis phototropin2 (phot2) [1]. In this study, photoregulation of the kinase in phototropin1 (phot1) was studied using LOV2-linker-kinase polypeptide. We designed a new substrate consisting of the N-terminal part of the phot1 with autophosphorylation sites. The LOV2-linker-kinase had the same spectroscopic properties as those of the LOV2 core and phosphorylated the substrate in a light-dependent manner. Amino acid substitution experiments proved that the phosphorylation comes from the activation of the kinase via photoreaction of LOV2.Structured summary of protein interactions:AtPhot1-LOV2 phosphorylates AtPhot1-Nt by protein kinase assay (View Interaction: 1, 2, 3