Identification of the cellulose synthase genes from the Oomycete Saprolegnia monoica and effect of cellulose synthesis inhibitors on gene expression and enzyme activity

Fungal Genet Biol. 2009 Oct;46(10):759-67. doi: 10.1016/j.fgb.2009.07.001. Epub 2009 Jul 7.

Abstract

Cellulose biosynthesis is a vital but yet poorly understood biochemical process in Oomycetes. Here, we report the identification and characterization of the cellulose synthase genes (CesA) from Saprolegnia monoica. Southern blot experiments revealed the occurrence of three CesA homologues in this species and phylogenetic analyses confirmed that Oomycete CesAs form a clade of their own. All gene products contained the D,D,D,QXXRW signature of most processive glycosyltransferases, including cellulose synthases. However, their N-terminal ends exhibited Oomycete-specific domains, i.e. Pleckstrin Homology domains, or conserved domains of an unknown function together with additional putative transmembrane domains. Mycelial growth was inhibited in the presence of the cellulose biosynthesis inhibitors 2,6-dichlorobenzonitrile or Congo Red. This inhibition was accompanied by a higher expression of all CesA genes in the mycelium and increased in vitro glucan synthase activities. Altogether, our data strongly suggest a direct involvement of the identified CesA genes in cellulose biosynthesis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Algal Proteins / genetics
  • Algal Proteins / metabolism
  • Blotting, Southern
  • Cellulose / biosynthesis*
  • Congo Red / pharmacology
  • DNA, Algal / genetics
  • Enzyme Inhibitors / pharmacology*
  • Gene Expression Regulation*
  • Glucosyltransferases / genetics*
  • Glucosyltransferases / metabolism*
  • Nitriles / pharmacology
  • Saprolegnia / drug effects*
  • Saprolegnia / enzymology*
  • Saprolegnia / genetics
  • Stress, Physiological

Substances

  • Algal Proteins
  • DNA, Algal
  • Enzyme Inhibitors
  • Nitriles
  • Congo Red
  • Cellulose
  • Glucosyltransferases
  • cellulose synthase
  • dichlobanil