Abstract

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 (H2O2) 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 H2O2 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.

Highlights

  • Plants face a variety of biotic stresses in nature, including bacteria and fungi, which can strongly affect growth and production [1]

  • The results of this study showed that AtPFA-DSP4 inhibited photosynthesis in all plants at 3 dpi, but the inhibition observed in OX8 and OX11 plants was reduced by approximately 29% and 41% compared with Col-0 (Figure 5A)

  • The results presented here show that OsPFA-DSP2 negatively regulates the pathogen response in rice

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Summary

Introduction

Plants face a variety of biotic stresses in nature, including bacteria and fungi, which can strongly affect growth and production [1]. The study by Asai et al [14] reported the identification of the components in a MAPK signalling pathway in Arabidopsis These authors demonstrated that in response to the flagellin-derived peptide flg, AtMEKK1 (a MAPKKKs) activates AtMKK4 and AtMKK5 (two MAPKKs), which in turn activate the functionally redundant MAPKs AtMPK3 and AtMPK6. This cascade results in transcription of defense-related genes, and was shown to play an important role in resistance to both bacterial and fungal pathogen [14]. Knockout mutants in AtMKP1 displayed elevated resistance to Pst DC3000 by regulating AtMPK6 activity, again suggesting that phosphatases play key roles in the biotic stresses response [20]

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