The Predicted Functional Compartmentation of Rice Terpenoid Metabolism by Trans-Prenyltransferase Structural Analysis, Expression and Localization

Int J Mol Sci. 2020 Nov 25;21(23):8927. doi: 10.3390/ijms21238927.

Abstract

Most terpenoids are derived from the basic terpene skeletons of geranyl pyrophosphate (GPP, C10), farnesyl-PP (FPP, C15) and geranylgeranyl-PP (GGPP, C20). The trans-prenyltransferases (PTs) mediate the sequential head-to-tail condensation of an isopentenyl-PP (C5) with allylic substrates. The in silico structural comparative analyses of rice trans-PTs with 136 plant trans-PT genes allowed twelve rice PTs to be identified as GGPS_LSU (OsGGPS1), homomeric G(G)PS (OsGPS) and GGPS_SSU-II (OsGRP) in Group I; two solanesyl-PP synthase (OsSPS2 and 3) and two polyprenyl-PP synthases (OsSPS1 and 4) in Group II; and five FPSs (OsFPS1, 2, 3, 4 and 5) in Group III. Additionally, several residues in "three floors" for the chain length and several essential domains for enzymatic activities specifically varied in rice, potentiating evolutionarily rice-specific biochemical functions of twelve trans-PTs. Moreover, expression profiling and localization patterns revealed their functional compartmentation in rice. Taken together, we propose the predicted topology-based working model of rice PTs with corresponding terpene metabolites: GPP/GGPPs mainly in plastoglobuli, SPPs in stroma, PPPs in cytosol, mitochondria and chloroplast and FPPs in cytosol. Our findings could be suitably applied to metabolic engineering for producing functional terpene metabolites in rice systems.

Keywords: functional compartmentation; in silico structural analysis; rice (Oryza sativa); subcellular localization; topology-based working model; trans-prenyltransferase.

MeSH terms

  • Dimethylallyltranstransferase / chemistry
  • Dimethylallyltranstransferase / genetics
  • Dimethylallyltranstransferase / ultrastructure*
  • Gene Expression Regulation, Plant
  • Oryza / chemistry
  • Oryza / genetics
  • Oryza / ultrastructure*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics
  • Plant Proteins / ultrastructure*
  • Polyisoprenyl Phosphates / chemistry
  • Polyisoprenyl Phosphates / metabolism
  • Protein Conformation
  • Structural Homology, Protein
  • Substrate Specificity
  • Terpenes / metabolism*

Substances

  • Plant Proteins
  • Polyisoprenyl Phosphates
  • Terpenes
  • geranyl pyrophosphate
  • Dimethylallyltranstransferase