Figure 1

Sequences of the GmRLK18-1 protein and the LRR domains expressed in E. coli . The whole RLK protein theoretical pI was 8.42 and the molecular weight was 92,388.98 Da. B. LRR domain fragment expressed in E. coli. Boxed was the peptide used to raise a specific antibody. In bold are the cysteine residue labeled by cross linking and the histidine residue polymorphic in resistant and susceptible plants. Boxed red is the trypsin fragment in contact with the cysteine when the homo-dimer forms; note it contains the histidine residue. The protein predicted pI was 9.54 and molecular weight 38,404.55 Da. Also shown was the amino acid sequence of the LRR domain of GmRLK08-1 near Rhg4 that was expressed in E. coli and used for ligand binding assays. The proteins predicted pI was 5.2 and molecular weight 38,086.11 Da. The LRR domain showed 45% similarity with that of GmRLK18-1.