Structural Characterization of a Eukaryotic Cyanase from Tetranychus urticae

J Agric Food Chem. 2017 Jul 12;65(27):5453-5462. doi: 10.1021/acs.jafc.7b01333. Epub 2017 Jun 30.

Abstract

The two-spotted spider mite Tetranychus urticae is a polyphagous agricultural pest and poses a high risk to global crop production as it is rapidly developing pesticide resistance. Genomic and transcriptomic analysis has revealed the presence of a remarkable cyanase gene in T. urticae and related mite species within the Acariformes lineage. Cyanase catalyzes the detoxification of cyanate and is potentially an attractive protein target for the development of new acaricides. Phylogenetic analysis indicates that within the Acariformes, the cyanase gene originates from a single horizontal gene transfer event, which precedes subsequent speciation. Our structural studies presented here compare and contrast prokaryotic cyanases to T. urticae cyanase, which all form homodecamers and have conserved active site residues, but display different surface areas between homodimers in the overall decameric structure.

Keywords: Tetranychus urticae; acaricides; agricultural pest; crystal structure; cyanase.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Arthropod Proteins / chemistry*
  • Arthropod Proteins / genetics
  • Arthropod Proteins / metabolism
  • Carbon-Nitrogen Lyases / chemistry*
  • Carbon-Nitrogen Lyases / genetics
  • Carbon-Nitrogen Lyases / metabolism
  • Molecular Sequence Data
  • Phylogeny
  • Protein Conformation
  • Sequence Alignment
  • Tetranychidae / chemistry
  • Tetranychidae / enzymology*
  • Tetranychidae / genetics

Substances

  • Arthropod Proteins
  • cyanate hydrolase
  • Carbon-Nitrogen Lyases