Fig. 5From: Conserved residues in the wheat (Triticum aestivum) NAM-A1 NAC domain are required for protein binding and when mutated lead to delayed peduncle and flag leaf senescenceMutations in the protein-binding domain of NAM-A1 inhibit protein binding. Yeast-two hybrid interaction screens between NAM-A1 alleles and wild-type NAM-B1 were tested on control (SC-LT; top row) and selective (SC-LTH + 10 mM 3AT; bottom row) media at ten-fold OD600 dilutions, from 10− 1 to 10− 5. Growth on selective media indicates interaction between the NAM-A1 allele and wild-type NAM-B1. Lack of growth on selective media indicates a loss of interaction. All controls showed equivalent growth on selective media as the wild-type NAM-A1 (purple). Left hand panels correspond to TILLING mutations whereas right hand panels are alanine substitutions. The corresponding TILLING line is shown underneath the mutation on the left panelBack to article page