Molecular cloning and characterization of a geranyl diphosphate-specific aromatic prenyltransferase from lemon

Plant Physiol. 2014 Sep;166(1):80-90. doi: 10.1104/pp.114.246892. Epub 2014 Jul 30.


Prenyl residues confer divergent biological activities such as antipathogenic and antiherbivorous activities on phenolic compounds, including flavonoids, coumarins, and xanthones. To date, about 1,000 prenylated phenolics have been isolated, with these compounds containing various prenyl residues. However, all currently described plant prenyltransferases (PTs) have been shown specific for dimethylallyl diphosphate as the prenyl donor, while most of the complementary DNAs encoding these genes have been isolated from the Leguminosae. In this study, we describe the identification of a novel PT gene from lemon (Citrus limon), ClPT1, belonging to the homogentisate PT family. This gene encodes a PT that differs from other known PTs, including flavonoid-specific PTs, in polypeptide sequence. This membrane-bound enzyme was specific for geranyl diphosphate as the prenyl donor and coumarin as the prenyl acceptor. Moreover, the gene product was targeted to plastid in plant cells. To our knowledge, this is the novel aromatic PT specific to geranyl diphosphate from citrus species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Citrus / enzymology*
  • Citrus / genetics
  • Dimethylallyltranstransferase / genetics
  • Dimethylallyltranstransferase / metabolism*
  • Diphosphates / metabolism*
  • Diterpenes / metabolism*
  • Molecular Sequence Data
  • Phylogeny
  • Plants, Genetically Modified
  • Plastids / metabolism
  • Ruta
  • Sequence Analysis, DNA
  • Sequence Homology, Nucleic Acid


  • Diphosphates
  • Diterpenes
  • geranyl diphosphate
  • Dimethylallyltranstransferase

Associated data

  • GENBANK/AB813876
  • GENBANK/AB813877