Publication detail

Involvement of an ent-copalyl diphosphate synthase in tissue-specific accumulation of specialized diterpenes in Andrographis paniculata

MISRA, R. GARG, A. ROY, S. CHANOTIYA, C. VASUDEV, P. GHOSH, S.

Original Title

Involvement of an ent-copalyl diphosphate synthase in tissue-specific accumulation of specialized diterpenes in Andrographis paniculata

Czech Title

Involvement of an ent-copalyl diphosphate synthase in tissue-specific accumulation of specialized diterpenes in Andrographis paniculata

English Title

Involvement of an ent-copalyl diphosphate synthase in tissue-specific accumulation of specialized diterpenes in Andrographis paniculata

Type

journal article

Language

en

Original Abstract

Ent-labdane-related diterpene (ent-LRD) specialized (i.e. secondary) metabolites of the medicinal plant kalmegh (Andrographis paniculata) have long been known for several pharmacological activities. However, our understanding of the ent-LRD biosynthetic pathway has remained largely incomplete. Since ent-LRDs accumulate in leaves, we carried out a comparative transcriptional analysis using leaf and root tissues, and identified 389 differentially expressed transcripts, including 223 transcripts that were preferentially expressed in leaf tissue. Analysis of the transcripts revealed various specialized metabolic pathways, including transcripts of the ent-LRD biosynthetic pathway. Two class II diterpene synthases (ApCPS1 and ApCPS2) along with one (ApCPS1) and two (ApCPS2 and ApCPS2) transcriptional variants that were the outcomes of alternative splicing of the precursor mRNA and alternative transcriptional termination, respectively, were identified. ApCPS1 and ApCPS2 encode for 832- and 817-amino acids proteins, respectively, and are phylogenetically related to the dicotyledons ent-copalyl diphosphate synthases (ent-CPSs). The spatio-temporal patterns of ent-LRD metabolites accumulation and gene expression suggested a likely role for ApCPS1 in general (i.e. primary) metabolism, perhaps by providing precursor for the biosynthesis of phytohormone gibberellin (GA). However, ApCPS2 is potentially involved in tissue-specific accumulation of ent-LRD specialized metabolites. Bacterially expressed recombinant ApCPS2 catalyzed the conversion of (E,E,E)-geranylgeranyl diphosphate (GGPP), the general precursor of diterpenes to ent-copalyl diphosphate (ent-CPP), the precursor of ent-LRDs. Taken together, these results advance

Czech abstract

Ent-labdane-related diterpene (ent-LRD) specialized (i.e. secondary) metabolites of the medicinal plant kalmegh (Andrographis paniculata) have long been known for several pharmacological activities. However, our understanding of the ent-LRD biosynthetic pathway has remained largely incomplete. Since ent-LRDs accumulate in leaves, we carried out a comparative transcriptional analysis using leaf and root tissues, and identified 389 differentially expressed transcripts, including 223 transcripts that were preferentially expressed in leaf tissue. Analysis of the transcripts revealed various specialized metabolic pathways, including transcripts of the ent-LRD biosynthetic pathway. Two class II diterpene synthases (ApCPS1 and ApCPS2) along with one (ApCPS1) and two (ApCPS2 and ApCPS2) transcriptional variants that were the outcomes of alternative splicing of the precursor mRNA and alternative transcriptional termination, respectively, were identified. ApCPS1 and ApCPS2 encode for 832- and 817-amino acids proteins, respectively, and are phylogenetically related to the dicotyledons ent-copalyl diphosphate synthases (ent-CPSs). The spatio-temporal patterns of ent-LRD metabolites accumulation and gene expression suggested a likely role for ApCPS1 in general (i.e. primary) metabolism, perhaps by providing precursor for the biosynthesis of phytohormone gibberellin (GA). However, ApCPS2 is potentially involved in tissue-specific accumulation of ent-LRD specialized metabolites. Bacterially expressed recombinant ApCPS2 catalyzed the conversion of (E,E,E)-geranylgeranyl diphosphate (GGPP), the general precursor of diterpenes to ent-copalyl diphosphate (ent-CPP), the precursor of ent-LRDs. Taken together, these results advance

English abstract

Ent-labdane-related diterpene (ent-LRD) specialized (i.e. secondary) metabolites of the medicinal plant kalmegh (Andrographis paniculata) have long been known for several pharmacological activities. However, our understanding of the ent-LRD biosynthetic pathway has remained largely incomplete. Since ent-LRDs accumulate in leaves, we carried out a comparative transcriptional analysis using leaf and root tissues, and identified 389 differentially expressed transcripts, including 223 transcripts that were preferentially expressed in leaf tissue. Analysis of the transcripts revealed various specialized metabolic pathways, including transcripts of the ent-LRD biosynthetic pathway. Two class II diterpene synthases (ApCPS1 and ApCPS2) along with one (ApCPS1) and two (ApCPS2 and ApCPS2) transcriptional variants that were the outcomes of alternative splicing of the precursor mRNA and alternative transcriptional termination, respectively, were identified. ApCPS1 and ApCPS2 encode for 832- and 817-amino acids proteins, respectively, and are phylogenetically related to the dicotyledons ent-copalyl diphosphate synthases (ent-CPSs). The spatio-temporal patterns of ent-LRD metabolites accumulation and gene expression suggested a likely role for ApCPS1 in general (i.e. primary) metabolism, perhaps by providing precursor for the biosynthesis of phytohormone gibberellin (GA). However, ApCPS2 is potentially involved in tissue-specific accumulation of ent-LRD specialized metabolites. Bacterially expressed recombinant ApCPS2 catalyzed the conversion of (E,E,E)-geranylgeranyl diphosphate (GGPP), the general precursor of diterpenes to ent-copalyl diphosphate (ent-CPP), the precursor of ent-LRDs. Taken together, these results advance

Keywords

Andrographis paniculata Ent-copalyl diphosphate synthase Ent-labdane-related diterpene Medicinal compound Specialized metabolism Transcriptional variants

RIV year

2015

Released

28.08.2015

Publisher

Elsevier

Location

UK

Pages from

50

Pages to

64

Pages count

16

BibTex


@article{BUT118101,
  author="Rajesh Chandra {Misra} and Anchal {Garg} and Sudeep {Roy} and Chandan Singh {Chanotiya} and Prema G. {Vasudev} and Sumit {Ghosh}",
  title="Involvement of an ent-copalyl diphosphate synthase in tissue-specific accumulation of specialized diterpenes in Andrographis paniculata",
  annote="Ent-labdane-related diterpene (ent-LRD) specialized (i.e. secondary) metabolites of the medicinal plant
kalmegh (Andrographis paniculata) have long been known for several pharmacological activities. However,
our understanding of the ent-LRD biosynthetic pathway has remained largely incomplete. Since
ent-LRDs accumulate in leaves, we carried out a comparative transcriptional analysis using leaf and root
tissues, and identified 389 differentially expressed transcripts, including 223 transcripts that were preferentially
expressed in leaf tissue. Analysis of the transcripts revealed various specialized metabolic
pathways, including transcripts of the ent-LRD biosynthetic pathway. Two class II diterpene synthases
(ApCPS1 and ApCPS2) along with one (ApCPS1) and two (ApCPS2 and ApCPS2) transcriptional variants that were the outcomes of alternative splicing of the precursor mRNA and alternative transcriptional termination,
respectively, were identified. ApCPS1 and ApCPS2 encode for 832- and 817-amino acids proteins,
respectively, and are phylogenetically related to the dicotyledons ent-copalyl diphosphate synthases
(ent-CPSs). The spatio-temporal patterns of ent-LRD metabolites accumulation and gene expression suggested
a likely role for ApCPS1 in general (i.e. primary) metabolism, perhaps by providing precursor for the
biosynthesis of phytohormone gibberellin (GA). However, ApCPS2 is potentially involved in tissue-specific
accumulation of ent-LRD specialized metabolites. Bacterially expressed recombinant ApCPS2 catalyzed
the conversion of (E,E,E)-geranylgeranyl diphosphate (GGPP), the general precursor of diterpenes to
ent-copalyl diphosphate (ent-CPP), the precursor of ent-LRDs. Taken together, these results advance",
  address="Elsevier",
  chapter="118101",
  doi="10.1016/j.plantsci.2015.08.016",
  howpublished="online",
  institution="Elsevier",
  number="240",
  year="2015",
  month="august",
  pages="50--64",
  publisher="Elsevier",
  type="journal article"
}