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

By Michael S. Bower, Ai Dinah D. Matias, Emily Fern, Maria Mazzurco, Tiesheng Gu, Steven J. Rothstein and Daphne R. Goringa

Abstract

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

Year: 2013
OAI identifier: oai:CiteSeerX.psu:10.1.1.318.1596
Provided by: CiteSeerX
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