JXB Advance Access originally published online on December 12, 2003
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Journal of Experimental Botany, Vol. 55, No. 396, pp. 535-537, February 1, 2004
© 2004 Oxford University Press
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Isolation and characterization of a Pti1 homologue from soybean
Received 10 July 2003; Accepted 9 October 2003
1 Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China
2 National Center for Soybean Improvement, Soybean Research Institute, Nanjing Agricultural University, Nanjing 210095, China
* To whom correspondence should be addressed: Fax: +86 10 6487 3428. E-mail: sychen{at}genetics.ac.cn; jszhang{at}genetics.ac.cn
A full-length gene GmPti1 was identified from soybean in an EST sequencing project by its homology to tomato Pti1. It encoded a protein of 366 amino acids. RT-PCR analysis showed that the GmPti1 expression was induced by salicylic acid and wounding. The deduced amino acid sequence had a Ser/Thr/Tyr kinase domain. GmPti1 protein was expressed in E. coli as an MBP fusion, purified by amylose resin and examined for its autophosphorylation ability. The phosphorylation assay in vitro showed that GmPti1 had kinase activity in the presence of Mn2+. These results demonstrated that GmPti1 represented a new Pti1-like gene, unlike the two published genes sPti1a and sPti1b, which encoding proteins had no autophosphorylation ability.
Key words: Autophosphorylation, GmPtil, kinase activity, soybean.