Comparative Study of Nonautolytic Mutant and Wild-Type Strains of Coprinopsis cinerea Supports an Important Role of Glucanases in Fruiting Body Autolysis

J Agric Food Chem. 2015 Nov 4;63(43):9609-14. doi: 10.1021/acs.jafc.5b03962. Epub 2015 Oct 20.

Abstract

Autolysis of Coprinopsis cinerea fruiting bodies affects its commercial value. In this study, a mutant of C. cinerea that exhibits pileus expansion without pileus autolysis was obtained using ultraviolet mutagenesis. This suggests that pileus expansion and pileus autolysis involve different enzymes or proteins. Among the detected hydrolytic enzymes, only β-1,3-glucanase activity increased with expansion and autolysis of pilei in the wild-type strain, but the increase was abolished in the mutant. This suggests that β-1,3-glucanases plays a major role in the autolysis. Although there are 43 possible β-1,3-glucoside hydrolases genes, only 4 known genes, which have products that are thought to act synergistically to degrade the β-1,3-glucan backbone of cell walls during fruiting body autolysis, and an unreported gene were upregulated during pileus expansion and autolysis in the wild-type stain but were suppressed in the mutant. This suggests that expression of these β-1,3-glucanases is potentially controlled by a single regulatory mechanism.

Keywords: Coprinopsis cinerea; fruiting body; pileus autolysis; pileus expansion; β-1,3-glucoside hydrolase.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Agaricales / enzymology*
  • Agaricales / genetics
  • Agaricales / growth & development
  • Agaricales / physiology*
  • Autolysis*
  • Fruiting Bodies, Fungal / enzymology*
  • Fruiting Bodies, Fungal / genetics
  • Fruiting Bodies, Fungal / growth & development
  • Fruiting Bodies, Fungal / physiology
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Expression Regulation, Fungal
  • Glycoside Hydrolases / genetics
  • Glycoside Hydrolases / metabolism*
  • Mutation

Substances

  • Fungal Proteins
  • Glycoside Hydrolases