Current Genetics

, Volume 59, Issue 1, pp 33–41

A serine/threonine-protein phosphatase PP2A catalytic subunit is essential for asexual development and plant infection in Magnaporthe oryzae

  • Yanxiu Du
  • Yang Shi
  • Jun Yang
  • Xiaolin Chen
  • Minfeng Xue
  • Wei Zhou
  • You-Liang Peng
Research Article

DOI: 10.1007/s00294-012-0385-3

Cite this article as:
Du, Y., Shi, Y., Yang, J. et al. Curr Genet (2013) 59: 33. doi:10.1007/s00294-012-0385-3

Abstract

Protein phosphatase 2A is a subgroup of widely conserved serine/threonine phosphatases and plays diverse roles in transcription, translation, differentiation, cell cycle, and signal transduction in many organisms. However, its roles in biotrophic and hemi-biotrophic phytopathogenic fungi remain to be investigated. In this study, we isolated an insertional mutant of the rice blast fungus Magnaporthe oryzae that was defective in vegetative hyphal growth. In the mutant, the T-DNA fragment was found to be inserted in the promoter region of a putative serine/threonine protein phosphatase 2A catalytic subunit (PP2Ac) gene MoPPG1. Deletion of MoPPG1 leads to severe defects in vegetative hyphal growth and conidiation. Conidia of the ∆Moppg1 null mutants were misshaped, and most of them were two-celled. The deletion mutants of MoPPG1 did not penetrate into host plant cells and failed to cause any disease lesions on rice leaves. Interestingly, significant reduction was found in the ∆Moppg1 null mutants in expression levels of several Rho GTPase family genes including MgCDC42, MgRHO3, and MgRAC1, which were important for pathogenesis of M. oryzae. Taken together, our results indicated that PP2Ac plays vital roles in asexual development and plant infection by regulating Rho GTPases in the rice blast fungus and perhaps other plant pathogenic fungi.

Keywords

ConidiationPathogenicityRice blast fungusSerine/threonine protein phosphataseVegetative hyphal growth

Supplementary material

294_2012_385_MOESM1_ESM.tif (1.3 mb)
Fig. S1 Alignment and phylogenetic tree of MoPpg1 with its orthologs. The alignment was generated with the ClustalX and ESPript programs using protein sequences MoPpg1 (Magnaporthe oryzae), EAA33034 (Neurospora crassa), EAK83067 (Ustilago maydis), Cpp1 (Fusarium verticillioides), CAK43262 (Aspergillus nidulans), SPAC22H10.04 (Schizosaccharomyces pombe), Ppg1 (Saccharomyces cerevisiae), pph1 (Sclerotinia sclerotiorium), PP2A-4 (Arabidopsis thaliana), PP2A-1 (Oryza sativa), PPH-4.1 (Caenorhabditis elegans), PP2AA (Homo sapiens). Identical residues among the sequences are marked in white within red shadow, and similar amino acids are marked in red within blue rectangle box. (TIFF 1324 kb)

Copyright information

© Springer-Verlag Berlin Heidelberg 2012

Authors and Affiliations

  • Yanxiu Du
    • 1
  • Yang Shi
    • 1
  • Jun Yang
    • 1
  • Xiaolin Chen
    • 1
  • Minfeng Xue
    • 1
  • Wei Zhou
    • 1
  • You-Liang Peng
    • 1
  1. 1.State Key Laboratory for Agrobiotechnology and Department of Plant PathologyChina Agricultural UniversityBeijingChina