Molecular chaperone function of Arabidopsis thaliana phloem protein 2-A1, encodes a protein similar to phloem lectin

被引:27
|
作者
Lee, Jung Ro [1 ,2 ,3 ]
Boltz, Kara A. [1 ]
Lee, Sang Yeol [2 ,3 ]
机构
[1] Texas A&M Univ, Dept Biochem & Biophys, College Stn, TX 77843 USA
[2] Gyeongsang Natl Univ, Div Appl Life Sci, Jinju 660701, South Korea
[3] Gyeongsang Natl Univ, PMBBRC, Jinju 660701, South Korea
关键词
Arabidopsis thaliana; Molecular chaperone; Antifungal activity; Phloem protein; Lectin; ANTIFUNGAL ACTIVITY; HEAT-SHOCK; ALPHA-CRYSTALLIN; FEEDING INSECTS; PLANTS; PATHOGEN; APHIDS; THIOREDOXIN; EXPRESSION; DEFENSE;
D O I
10.1016/j.bbrc.2013.11.034
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
Although several phloem sap proteins have been identified from protein extracts of heat-treated Arabidopsis seedlings using FPLC gel filtration columns, many of the physiological roles played by these proteins remain to be elucidated. We functionally characterized a phloem protein 2-A1, which encodes a protein similar to phloem lectin. Using a bacterially expressed recombinant protein of AtPP2-A1, we found that it performs dual functions, showing both molecular chaperone activity and antifungal activity. mRNA expression of the AtPP2-1 gene was induced by diverse external stresses such as pathogens, and other signaling molecules, such as ethylene. These results suggest that the AtPP2-A1 molecular chaperone protein plays a critical role in the Arabidopsis defense system against diverse external stresses including fungal pathogenic attack and heat shock. (C) 2013 Elsevier Inc. All rights reserved.
引用
收藏
页码:18 / 21
页数:4
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