Isolation and characterization of NgRLK1, a receptor-like kinase of Nicotiana glutinosa that interacts with the elicitin of Phytophthora capsici

被引：34

作者：

Kim, Yeong-Tae ^{[1
]}

Oh, Jonghee ^{[1
]}

Kim, Kyung-Hwan ^{[1
]}

Uhm, Jae-Youl ^{[2
]}

Lee, Byoung-Moo ^{[1
]}

机构：

[1] Rural Dev Adm, Natl Inst Agr Sci, Suwon 441707, South Korea

[2] Kyungpook Natl Univ, Div Appl Biol & Chem, Taegu 702701, South Korea

来源：

MOLECULAR BIOLOGY REPORTS | 2010年 / 37卷 / 02期

关键词：

Phytophthora capsici; Elicitin; Capsicein; HR; RLK; NgRLK1; PROTEIN-KINASE; ARABIDOPSIS-THALIANA; GENE-CLUSTER; TOBACCO; RESISTANCE; CRYPTOGEIN; IDENTIFICATION; AUTOPHOSPHORYLATION; RECOGNITION; SEQUENCE;

D O I：

10.1007/s11033-009-9570-y

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Elicitins, extracellular proteins from Phytophthora fungi, elicit a hypersensitivity response (HR), including systemic acquired resistance, in some plants. The elicitin capsicein (similar to 10 kDa) was purified by FPLC from culture filtrates of P. capsici. Purified native and recombinant capsicein induced a hypersensitive response in leaves of the non-host plants Nicotiana glutinosa and Brassica rapa subsp. pekinensis. To search for candidate capsicein-interacting proteins from N. glutinosa, a yeast two-hybrid assay was used. We identified a protein interactor that is homologous to a serine/threonine kinase of the plant receptor-like kinase (RLK) group and designated it NgRLK1. The ORF of NgRLK1 encodes a polypeptide of 832 amino acids (93,490 Da). A conserved domain analysis revealed that NgRLK1 has structural features typical of a plant RLK. NgRLK1 was autophosphorylated, with higher activity in the presence of Mn2+ than Mg2+.

引用

页码：717 / 727

页数：11

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