Isolation and characterization of a Pti1 homologue from soybean

• Published in: Journal of experimental botany 2004-02, Vol.55 (396), p.535-537
• Main Authors: Tian, Ai‐Guo, Luo, Guang‐Zuo, Wang, Yong‐Jun, Zhang, Jin‐Song, Gai, Jun‐Yi, Chen, Shou‐Yi
• Format: Article
• Language: English
• Subjects: Agronomy. Soil science and plant productions; Amino Acid Sequence; Amino acids; Autophosphorylation; Base Sequence; Biological and medical sciences; Classical and quantitative genetics. Population genetics. Molecular genetics; DNA Primers; Fundamental and applied biological sciences. Psychology; Gels; Gene Notes; Generalities. Genetics. Plant material; Genes; Genes. Genome; Genetics and breeding of economic plants; Glycine max - enzymology; Glycine max - genetics; GmPtil; kinase activity; Molecular and cellular biology; Molecular genetics; Pathogens; Plant Proteins; Plants; Polymerase Chain Reaction; Protein Serine-Threonine Kinases - genetics; Protein Serine-Threonine Kinases - isolation & purification; Protein Serine-Threonine Kinases - metabolism; Reverse transcriptase polymerase chain reaction; RNA; Seedlings; Sequence Homology, Amino Acid; soybean; Soybeans
• ISSN: 0022-0957; 1460-2431
• DOI: 10.1093/jxb/erh035

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.