Identification of three clones which commonly interact with the kinase domains of highly homologous two receptor-like kinases, RLK902 and RKL1.

We have previously reported the characterization of highly homologous two leucine-rich repeat (LRR)-receptor-like kinase (RLK) genes, RLK902 and RKL1, which showed 75% identity at the amino acid sequence level. To investigate the RLK902 and RKL1 mediated signal transduction pathways, we performed yeast two-hybrid screening using the kinase domains of RLK902 and RKL1 as baits. Three clones, Y-1, 2 and 3, were found to interact commonly with the kinase domain of RLK902 and RKL1 and not to interact with the kinase domain of BRI1, a member of LRR-RLKs. This result suggests that RLK902 and RKL1 may have common biochemical functions, especially in their downstream signal transduction. Furthermore, the detail analysis of their responsiveness to various conditions suggests their involvement in such stress conditions as mechanical wounding, treatment with salicylic acid, and pathogen infection.
Mesh Terms:
Arabidopsis, Arabidopsis Proteins, Binding Sites, Cloning, Molecular, Gene Expression Regulation, Plant, Plant Diseases, Protein Binding, Protein Kinases, Protein Structure, Tertiary, Pseudomonas syringae, Salicylic Acid, Signal Transduction, Two-Hybrid System Techniques
Biosci. Biotechnol. Biochem. Dec. 01, 2004; 68(12);2581-7 [PUBMED:15618630]
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