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. 1996 Sep;8(9):1641–1650. doi: 10.1105/tpc.8.9.1641

Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase.

M S Bower 1, D D Matias 1, E Fernandes-Carvalho 1, M Mazzurco 1, T Gu 1, S J Rothstein 1, D R Goring 1
PMCID: PMC161304  PMID: 8837514

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.

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Selected References

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