The Putative Histone Methyltransferase DOT1 Regulates Aflatoxin and Pathogenicity Attributes in Aspergillus flavus

Toxins (Basel). 2017 Jul 24;9(7):232. doi: 10.3390/toxins9070232.

Abstract

Lysine methyltransferases transfer methyl groups in specific lysine sites, which regulates a variety of important biological processes in eukaryotes. In this study, we characterized a novel homolog of the yeast methyltransferase DOT1 in A. flavus, and observed the roles of dot1 in A. flavus. Deletion of dot1 showed a significant decrease in conidiation, but an increase in sclerotia formation. A change in viability to multiple stresses was also found in the Δdot1 mutant. Additionally, aflatoxin (AF) production was found severely impaired in the Δdot1 mutant. Further analysis by qRT-PCR revealed that the transcription of AF structural genes and their regulator gene aflS were prominently suppressed in the Δdot1 mutant. Furthermore, our data revealed that Dot1 is important for colonizing maize seeds in A. flavus. Our research indicates that Dot1 is involved in fungal development, aflatoxin biosynthesis and fungal virulence in A. flavus, which might provide a potential target for controlling A. flavus with new strategies.

Keywords: fungal virulence; histone methylation; sclerotia; stress response.

MeSH terms

  • Aflatoxins / biosynthesis*
  • Aspergillus flavus / genetics
  • Aspergillus flavus / growth & development
  • Aspergillus flavus / metabolism*
  • Aspergillus flavus / pathogenicity*
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase / genetics
  • Histone-Lysine N-Methyltransferase / metabolism*
  • Seeds / microbiology
  • Spores, Fungal / growth & development
  • Virulence
  • Zea mays / microbiology

Substances

  • Aflatoxins
  • Fungal Proteins
  • Histone Methyltransferases
  • Histone-Lysine N-Methyltransferase