Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae)
2023
Аутори:
Aničić, NedaMatekalo, Dragana
Skorić, Marijana
Gašić, Uroš
Nestorović Živković, Jasmina
Dmitrović, Slavica
Božunović, Jelena
Milutinović, Milica
Petrović, Luka
Dimitrijević, Milena
Anđelković, Boban
Mišić, Danijela
Тип документа:
Чланак у часопису (Објављена верзија)
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© 2024 Aničić, Matekalo, Skorić, Gašić, Nestorović Živković, Dmitrović, Božunović, Milutinović, Petrović, Dimitrijević, Anđelković and Mišić.
Метаподаци
Приказ свих података о документуАпстракт:
Iridoids, a class of atypical monoterpenes, exhibit exceptional diversity within the Nepeta genus (subfam. Nepetoidae, fam. Lamiaceae).The majority of these plants produce iridoids of the unique stereochemistry, with nepetalactones (NLs) predominating; however, a few Nepeta species lack these compounds. By comparatively analyzing metabolomics, transcriptomics, gene co-expression, and phylogenetic data of the iridoid-producing N. rtanjensis Diklić & Milojević and iridoid-lacking N. nervosa Royle & Bentham, we presumed that one of the factors responsible for the absence of these compounds in N. nervosa is iridoid synthase (ISY). Two orthologues of ISY were mined from leaves transcriptome of N. rtanjensis (NrPRISE1 and NrPRISE2), while in N. nervosa only one (NnPRISE) was identified, and it was phylogenetically closer to the representatives of the Family 1 isoforms, designated as P5βRs. Organ-specific and MeJA-elicited profiling of iridoid content and co-expression analysis of IBG candidates, highlighted NrPRISE2 and NnPRISE as promising candidates for ISY orthologues, and their function was confirmed using in vitro assays with recombinant proteins, after heterologous expression of recombinant proteins in E. coli and their His-tag affinity purification. NrPRISE2 demonstrated ISY activity both in vitro and likely in planta, which was supported by the 3D modeling and molecular docking analysis, thus reclassification of NrPRISE2 to NrISY is accordingly recommended. NnPRISE also displays in vitro ISY-like activity, while its role under in vivo conditions was not here unambiguously confirmed. Most probably under in vivo conditions the NnPRISE lacks substrates to act upon, as a result of the loss of function of some of the upstream enzymes of the iridoid pathway. Our ongoing work is conducted towards re-establishing the biosynthesis of iridoids in N. nervosa.
Напомена:
Paper published in 2024
Кључне речи:
iridoid synthase; iridoids; Nepeta rtanjensis; Nepeta nervosa; functional characterization; metabolomics; transcriptomicsИзвор:
Frontiers in Plant Science, 2023, 14, 1211453-Финансирање / пројекти:
- Министарство науке, технолошког развоја и иновација Републике Србије, институционално финансирање - 200007 (Универзитет у Београду, Институт за биолошка истраживања 'Синиша Станковић') (RS-MESTD-inst-2020-200007)
- NEPETOME - Omics-guided disentangling of the iridoid diversity in the genus Nepeta L. for in planta metabolic engineering towards sustainable exploitation (RS-ScienceFundRS-Ideje-7749433)
DOI: 10.3389/fpls.2023.1211453
ISSN: 1664-462X
PubMed: 38235204