Molecular Cloning and Characterisation of Farnesyl Pyrophosphate Synthase from Tripterygium wilfordii

PLoS One. 2015 May 4;10(5):e0125415. doi: 10.1371/journal.pone.0125415. eCollection 2015.

Abstract

Farnesylpyrophosphate synthase (FPS) catalyzes the biosynthesis of farnesyl pyrophosphate (FPP), which is an important precursor of sesquiterpenoids such as artemisinin and wilfordine. In the present study, we report the molecular cloning and characterization of two full-length cDNAs encoding FPSs from Tripterygium wilfordii (TwFPSs). TwFPSs maintained their capability to synthesise FPP in vitro when purified as recombinant proteins from E. coli. Consistent with the endogenous role of FPS in FPP biosynthesis, TwFPSs were highly expressed in T. wilfordii roots, and were up-regulated upon methyl jasmonate (MeJA) treatment. The global gene expression profiles suggested that the TwFPSs might play an important regulatory role interpenoid biosynthesis in T. wilfordii, laying the groundwork for the future study of the synthetic biology of natural terpene products.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetates / pharmacology
  • Amino Acid Sequence
  • Biocatalysis / drug effects
  • Cloning, Molecular
  • Cyclopentanes / pharmacology
  • DNA, Complementary / genetics
  • Electrophoresis, Polyacrylamide Gel
  • Gas Chromatography-Mass Spectrometry
  • Gene Expression Profiling
  • Gene Expression Regulation, Plant / drug effects
  • Geranyltranstransferase / chemistry
  • Geranyltranstransferase / genetics*
  • Geranyltranstransferase / metabolism
  • Molecular Sequence Data
  • Organ Specificity / drug effects
  • Organ Specificity / genetics
  • Oxylipins / pharmacology
  • Phylogeny
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / metabolism
  • Recombinant Proteins / metabolism
  • Tripterygium / enzymology*
  • Tripterygium / genetics

Substances

  • Acetates
  • Cyclopentanes
  • DNA, Complementary
  • Oxylipins
  • Plant Proteins
  • Recombinant Proteins
  • methyl jasmonate
  • Geranyltranstransferase

Associated data

  • GENBANK/KM058711
  • GENBANK/KM058712

Grants and funding

This work was supported by the National Natural Science Foundation of China (81422053 and 81373906 to WG, and 81325023 to LH) and the Author of National Excellent Doctoral Dissertation of China (201188) and the Importation and Development of High-Caliber Talents Project of Beijing Municipal Institutions (CIT&TCD201304174) to WG.