THE PLANT CELL, Vol 8, Issue 9 1641-1650, Copyright © 1996 by American Society of Plant Biologists

RESEARCH ARTICLES

Two Members of the Thioredoxin-h Family Interact with the Kinase Domain of a Brassica S Locus Receptor Kinase

M. S. Bower, D. D. Matias, E. Fernandes-Carvalho, M. Mazzurco, T. Gu, S. J. Rothstein and D. R. Goring
Biology Department, York University, 4700 Keele Street, North York, Ontario, M3J 1P3 Canada

To determine potential targets of the S locus receptor kinase (SRK) during the Brassica self-incompatibility response, a yeast two-hybrid library was screened with the SRK-910 protein kinase domain. Two thioredoxin-h-like clones, THL-1 and THL-2, were found to interact specifically with the SRK-910 protein kinase domain and not to interact with the protein kinase domains from the Arabidopsis receptor-like protein kinases (RLK) RLK4 and RLK5. The interaction between THL-1 and the SRK-910 protein kinase domain was confirmed using coimmunoprecipitation experiments with fusion proteins produced in Escherichia coli. THL-1 has thioredoxin activity based on an insulin reduction assay, and THL-1 is weakly phosphorylated by the SRK-910 protein kinase domain. THL-1 and THL-2 are both expressed in a variety of tissues but show some differences in steady state mRNA levels, with THL-2 being preferentially expressed in floral tissues. This indicates a more general biological function for these thioredoxins in addition to a potential role as effector molecules in the self-incompatibility signal cascade.

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