Isolation and characterization of a Pti1 homologue from soybean | Zendy

Aiguo Tian | Zendy; Guangzuo Luo | Zendy; Yongjun Wang | Zendy; JinSong Zhang | Zendy; Gai Junyi | Zendy; Shouyi Chen | Zendy

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Isolation and characterization of a Pti1 homologue from soybean

Author(s) -

Aiguo Tian,

Guangzuo Luo,

Yongjun Wang,

JinSong Zhang,

Gai Junyi,

Shouyi Chen

Publication year - 2004

Publication title -

journal of experimental botany

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.616

H-Index - 242

eISSN - 1460-2431

pISSN - 0022-0957

DOI - 10.1093/jxb/erh035

Subject(s) - autophosphorylation , gene , biochemistry , amino acid , biology , homology (biology) , microbiology and biotechnology , peptide sequence , fusion protein , protein kinase domain , kinase , protein kinase a , chemistry , recombinant dna , mutant

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.

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