Ustiloxins, fungal cyclic peptides, are ribosomally synthesized in Ustilaginoidea virens

Bioinformatics. 2015 Apr 1;31(7):981-5. doi: 10.1093/bioinformatics/btu753. Epub 2014 Nov 19.

Abstract

Motivation: Ustiloxins A and B are toxic cyclic tetrapeptides, Tyr-Val/Ala-Ile-Gly (Y-V/A-I-G), that were originally identified from Ustilaginoidea virens, a pathogenic fungus affecting rice plants. Contrary to our report that ustiloxin B is ribosomally synthesized in Aspergillus flavus, a recent report suggested that ustiloxins are synthesized by a non-ribosomal peptide synthetase in U.virens. Thus, we analyzed the U.virens genome, to identify the responsible gene cluster.

Results: The biosynthetic gene cluster was identified from the genome of U.virens based on homologies to the ribosomal peptide biosynthetic gene cluster for ustiloxin B identified from A.flavus. It contains a gene encoding precursor protein having five Tyr-Val-Ile-Gly and three Tyr-Ala-Ile-Gly motifs for ustiloxins A and B, respectively, strongly indicating that ustiloxins A and B from U.virens are ribosomally synthesized.

Availability and implementation: Accession codes of the U.virens and A.flavus gene clusters in NCBI are BR001221 and BR001206, respectively. Supplementary data are available at Bioinformatics online.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Biosynthetic Pathways
  • Fungal Proteins / biosynthesis
  • Fungal Proteins / genetics*
  • Genes, Fungal*
  • Genome, Fungal
  • Molecular Sequence Data
  • Multigene Family*
  • Peptides, Cyclic / biosynthesis
  • Peptides, Cyclic / genetics*
  • Ribosomes / metabolism*
  • Sequence Analysis, DNA / methods
  • Sequence Homology, Amino Acid
  • Ustilago / genetics*
  • Ustilago / growth & development
  • Ustilago / metabolism

Substances

  • Fungal Proteins
  • Peptides, Cyclic
  • ustiloxin B
  • ustiloxin A