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Quantitative label-free phosphoproteomics of six different life stages of the late blight pathogen Phytophthora infestans reveals abundant phosphorylation of members of the CRN effector family

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  • Svante Resjö
  • Ashfaq Ali
  • Harold J G Meijer
  • Michael F Seidl
  • Berend Snel
  • Marianne Sandin
  • Fredrik Levander
  • Francine Govers
  • Erik Andreasson
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The oomycete Phytophthora infestans is the causal agent of late blight in potato and tomato. Since the underlying processes that govern pathogenicity and development in P. infestans are largely unknown, we have performed a large-scale phosphoproteomics study of six different P. infestans life stages. We have obtained quantitative data for 2922 phosphopeptides and compared their abundance. Life-stage-specific phosphopeptides include ATP-binding cassette transporters and a kinase that only occurs in appressoria. In an extended data set, we identified 2179 phosphorylation sites and deduced 22 phosphomotifs. Several of the phosphomotifs matched consensus sequences of kinases that occur in P. infestans but not Arabidopsis. In addition, we detected tyrosine phosphopeptides that are potential targets of kinases resembling mammalian tyrosine kinases. Among the phosphorylated proteins are members of the RXLR and Crinkler effector families. The latter are phosphorylated in several life stages and at multiple positions, in sites that are conserved between different members of the Crinkler family. This indicates that proteins in the Crinkler family have functions beyond their putative role as (necrosis-inducing) effectors. This phosphoproteomics data will be instrumental for studies on oomycetes and host-oomycete interactions. The data sets have been deposited to ProteomeXchange (identifier PXD000433).

Original languageEnglish
JournalJournal of Proteome Research
Issue number4
Pages (from-to)1848-59
Number of pages12
Publication statusPublished - 4 Apr 2014
Externally publishedYes

    Research areas

  • Amino Acid Motifs, Amino Acid Sequence, Life Cycle Stages, Molecular Sequence Data, Phosphopeptides, Phosphoproteins, Phosphorylation, Phytophthora infestans, Protein-Serine-Threonine Kinases, Proteomics, Tissue Culture Techniques, Journal Article, Research Support, Non-U.S. Gov't

ID: 53678829