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Protein phosphatases, together with protein kinases, regulate protein phosphorylation and dephosphorylation, and play critical roles in plant growth and biotic stress responses. However, little is known about the biological functions of plant protein tyrosine dual-specificity phosphatase (PFA-DSP) in biotic stresses. Here, we found that  OsPFA-DSP2  was mainly expressed in calli, seedlings, roots, and young panicles, and localized in cytoplasm and nucleus. Ectopic overexpression of  OsPFA-DSP2  in rice increased sensitivity to  Magnaporthe grisea  ( M. grisea  Z1 strain), inhibited the accumulation of hydrogen peroxide (H 2 O 2 ) and suppressed the expression of pathogenesis-related ( PR ) genes after fungal infection. Interestingly, transgenic Arabidopsis plants overexpressing  AtPFA-DSP4 , which is homologous to  OsPFA-DSP2 , also exhibited sensitivity to  Pseudomonas syringae  pv.  tomato  DC3000 ( Pst  DC3000), reduced accumulation of H 2 O 2  and decreased photosynthesic capacity after infection compared with Col-0. These results indicate that OsPFA-DSP2 and AtPFA-DSP4 act as negative regulators of the pathogen response in transgenic plants.

Two Homologous Putative Protein Tyrosine Phosphatases, OsPFA-DSP2 and AtPFA-DSP4, Negatively Regulate the Pathogen Response in Transgenic Plants