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J. Biol. Chem., Vol. 280, Issue 10, 9203-9209, March 11, 2005

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Regulation of Plant Symbiosis Receptor Kinase through Serine and Threonine Phosphorylation^*

Satoko Yoshida and Martin Parniske

From the Sainsbury Laboratory, John Innes Centre, Colney Lane, Norwich, NR4 7UH, United Kingdom

We studied the biochemical properties of a plant receptor-like kinase to gain insights into the regulatory mechanism of this largest class of plant kinases. SYMRK (symbiosis receptor kinase) is required for early signal transduction leading to plant root symbioses with nitrogen-fixing rhizobia and phosphate-acquiring arbuscular mycorrhizal fungi. Amino acid substitutions in positions critical for activity of other related kinases cause a nonsymbiotic plant phenotype, suggesting that SYMRK kinase activity is required for symbiosis. SYMRK is capable of intermolecular autophosphorylation. Nonphosphorylated SYMRK is less active than the phosphorylated version, suggesting the phosphorylation status of SYMRK determines its activity. Three Ser/Thr residues were identified as residues required for full kinase activation through targeted mutagenesis. Using quadrupole time-of-flight mass spectrometry analysis, two of these were confirmed to be phosphorylated in vitro. These crucial phosphorylation sites are conserved among various plant receptor-like kinases as well as animal Pelle/interleukin-1 receptor associated kinase. Despite the distinct domain architecture of receptor-like kinases versus Pelle/interleukin-1 receptor associated kinase, our results suggest the existence of conserved activation mechanisms.

Received for publication, October 13, 2004 , and in revised form, November 26, 2004.

^* This work was funded by Biotechnology and Biological Sciences Research Council, Swindon, United Kingdom Grant 83/P18240. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Present address: Genetics Institute, Ludwig Maximilians Universität (LMU), Maria-Ward-Strasse 1a, D-80638 München, Germany. Tel.: 49-89-2180-6188; Fax: 49-89-2180-6169; E-mail: satoko.yoshida{at}lrz.uni-muenchen.de. To whom correspondence should be addressed: Genetics Institute, Ludwig Maximilians Universität (LMU), Maria-Ward-Strasse 1a, D-80638 München, Germany. Tel.: 49-89-2180-6150; Fax: 49-89-1785633; E-mail: martin.parniske{at}lrz.uni-muenchen.de.

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