3 years ago

Loss of chloroplast localized protein phosphatase 2Cs in Arabidopsis thaliana leads to enhancement of the plant immunity and resistance to Xanthomonas campestris pv. campestris infection

Hirokazu Ochiai, Chiharu Akimoto-Tomiyama, Eiichi Minami, Hideyuki Kajiwara, Shigeru Tanabe
Protein phosphatases (PPs) counteract kinases in reversible phosphorylation events during numerous signal transduction pathways in eukaryotes. PP2Cs, one of the four major classes of serine/threonine specific PPs family is greatly expanded in plants. Thus PP2C is thought to have a specific role in a signal transduction pathway. Some rice PP2Cs classified to subgroup K were responsive to the infection by the compatible Xanthomonas oryzae pv. oryzae, the causal agent of bacterial blight. In A. thaliana, orthologous PP2C genes (AtPP2C62 and AtPP2C26) classified to subgroup K were also responsive to Xanthomonas campestris pv. campestris (Xcc, causal agent of the Black rot) infection. To elucidate the function of these subgroup K PP2Cs, atpp2c62 and atpp2c26 deficient A. thaliana mutants were characterized. A double mutant plant which was inoculated with a compatible Xcc showed reduced lesion development as well as the suppression of bacterial multiplication. AtPP2C62 and AtPP2C26 localized to the chloroplast. Furthermore, photosynthesis related proteins, chaperonin-60 was indicated as the potent candidate for de-phosphorylated substrate catalyzed by AtPP2C62 and AtPP2C26 using the 2D-IDF-SDS-PAGE method. Taken together, AtPP2C62 and AtPP2C26 are suggested to be involved in both photosynthesis and suppression of plant immune system. These results imply the occurrence of the crosstalk between photosynthesis and the plant defense system to control the productivity under pathogen infection. This article is protected by copyright. All rights reserved.

Publisher URL: http://onlinelibrary.wiley.com/resolve/doi

DOI: 10.1111/mpp.12596

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