Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

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

Resjo, Svante ; Ali, Ashfaq ; Meijer, Harold J. G. ; Seidl, Michael F. ; Snel, Berend ; Sandin, Marianne LU ; Levander, Fredrik LU orcid ; Govers, Francine and Andreasson, Erik (2014) In Journal of Proteome Research 13(4). p.1848-1859
Abstract
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-stages-pecific 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... (More)
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-stages-pecific 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). (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
Phytophthora infestans, late blight, potato, protein phosphorylation, proteomics, phosphoproteomics, effectors, Crinklers, CRN proteins, tyrosine phosphorylation, phosphorylation motifs, appressorium
in
Journal of Proteome Research
volume
13
issue
4
pages
1848 - 1859
publisher
The American Chemical Society (ACS)
external identifiers
  • wos:000334016400007
  • scopus:84898755900
  • pmid:24588563
ISSN
1535-3893
DOI
10.1021/pr4009095
language
English
LU publication?
yes
id
5edb98c4-b723-4b85-bf02-4f73ff04145c (old id 4439624)
date added to LUP
2016-04-01 10:01:58
date last changed
2024-06-30 07:49:29
@article{5edb98c4-b723-4b85-bf02-4f73ff04145c,
  abstract     = {{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-stages-pecific 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).}},
  author       = {{Resjo, Svante and Ali, Ashfaq and Meijer, Harold J. G. and Seidl, Michael F. and Snel, Berend and Sandin, Marianne and Levander, Fredrik and Govers, Francine and Andreasson, Erik}},
  issn         = {{1535-3893}},
  keywords     = {{Phytophthora infestans; late blight; potato; protein phosphorylation; proteomics; phosphoproteomics; effectors; Crinklers; CRN proteins; tyrosine phosphorylation; phosphorylation motifs; appressorium}},
  language     = {{eng}},
  number       = {{4}},
  pages        = {{1848--1859}},
  publisher    = {{The American Chemical Society (ACS)}},
  series       = {{Journal of Proteome Research}},
  title        = {{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}},
  url          = {{http://dx.doi.org/10.1021/pr4009095}},
  doi          = {{10.1021/pr4009095}},
  volume       = {{13}},
  year         = {{2014}},
}