Phosphoproteome profiles of the phytopathogenic fungi Alternaria brassicicola and Botrytis cinerea during exponential growth in axenic cultures

Proteomics. 2014 Jul;14(13-14):1639-45. doi: 10.1002/pmic.201300541. Epub 2014 Jun 16.

Abstract

This study describes the gel-free phosphoproteomic analysis of the phytopathogenic fungi Alternaria brassicicola and Botrytis cinerea grown in vitro under nonlimiting conditions. Using a combination of strong cation exchange and IMAC prior to LC-MS, we identified over 1350 phosphopeptides per fungus representing over 800 phosphoproteins. The preferred phosphorylation sites were found on serine (>80%) and threonine (>15%), whereas phosphorylated tyrosine residues were found at less than 1% in A. brassicicola and at a slightly higher ratio in B. cinerea (1.5%). Biological processes represented principally among the phoshoproteins were those involved in response and transduction of stimuli as well as in regulation of cellular and metabolic processes. Most known elements of signal transduction were found in the datasets of both fungi. This study also revealed unexpected phosphorylation sites in histidine kinases, a category overrepresented in filamentous ascomycetes compared to yeast. The data have been deposited to the ProteomeXchange database with identifier PXD000817 (http://proteomecentral.proteomexchange.org/dataset/PXD000817).

Keywords: Black spot; Gray mold; Microbiology; PTMs; Protein phosphorylation; Signal transduction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alternaria / chemistry
  • Alternaria / growth & development*
  • Alternaria / metabolism
  • Amino Acid Sequence
  • Axenic Culture
  • Botrytis / chemistry
  • Botrytis / growth & development*
  • Botrytis / metabolism
  • Fungal Proteins / chemistry
  • Fungal Proteins / metabolism*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Phosphoproteins / chemistry
  • Phosphoproteins / metabolism*
  • Proteomics
  • Signal Transduction

Substances

  • Fungal Proteins
  • Phosphoproteins