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Updated: May 5, 2026

Collection and Analysis of Arabidopsis Phloem Exudates Using the EDTA-facilitated Method
Published on: October 23, 2013
Molecular chaperone function of Arabidopsis thaliana phloem protein 2-A1, encodes a protein similar to phloem lectin
Jung Ro Lee1, Kara A Boltz2, Sang Yeol Lee3
1Department of Biochemistry and Biophysics, Texas A&M University, College Station, TX 77843, USA; Division of Applied Life Sciences and PMBBRC, Gyeongsang National University, Jinju 660-701, Republic of Korea.
Abstract:
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.
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