The molecular basis of resistance to the herbicide norflurazon

Plant Mol Biol. 1991 Jun;16(6):967-74. doi: 10.1007/BF00016069.

Abstract

We have cloned and sequenced a gene, pds, from the cyanobacterium Synechococcus PCC7942 that is responsible for resistance to the bleaching herbicide norflurazon. A point mutation in that gene, leading to an amino acid substitution from valine to glycine in its polypeptide product, was found to confer this resistance. Previous studies with herbicide-resistant mutants have indicated that this gene encodes phytoene desaturase (PDS), a key enzyme in the biosynthesis of carotenoids. A short amino acid sequence that is homologous to conserved motifs in the binding sites for NAD(H) and NADP(H) was identified in PDS, suggesting the involvement of these dinucleotides as cofactors in phytoene desaturation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites / genetics
  • Cloning, Molecular
  • Cyanobacteria / drug effects
  • Cyanobacteria / enzymology
  • Cyanobacteria / genetics*
  • DNA Mutational Analysis
  • Drug Resistance, Microbial / genetics
  • Herbicides / metabolism
  • Herbicides / pharmacology*
  • Molecular Sequence Data
  • NAD / metabolism
  • Oxidoreductases / chemistry
  • Oxidoreductases / genetics*
  • Oxidoreductases / metabolism
  • Pyridazines / metabolism
  • Pyridazines / pharmacology*
  • Restriction Mapping
  • Sequence Homology, Nucleic Acid

Substances

  • Herbicides
  • Pyridazines
  • NAD
  • Oxidoreductases
  • phytoene dehydrogenase
  • norflurazone

Associated data

  • GENBANK/X55289