TY  - JOUR
AU  - Aničić, Neda
AU  - Matekalo, Dragana
AU  - Skorić, Marijana
AU  - Gašić, Uroš M.
AU  - Nestorović Živković, Jasmina
AU  - Dmitrović, Slavica
AU  - Božunović, Jelena
AU  - Milutinović, Milica
AU  - Petrović, Luka
AU  - Dimitrijević, Milena
AU  - Anđelković, Boban D.
AU  - Mišić, Danijela
PY  - 2024
UR  - http://cherry.chem.bg.ac.rs/handle/123456789/6454
AB  - 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.
PB  - Frontiers Media
T2  - Frontiers in Plant Science
T1  - Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae)
VL  - 14
DO  - 10.3389/fpls.2023.1211453
ER  - 

@article{
author = "Aničić, Neda and Matekalo, Dragana and Skorić, Marijana and Gašić, Uroš M. and Nestorović Živković, Jasmina and Dmitrović, Slavica and Božunović, Jelena and Milutinović, Milica and Petrović, Luka and Dimitrijević, Milena and Anđelković, Boban D. and Mišić, Danijela",
year = "2024",
abstract = "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.",
publisher = "Frontiers Media",
journal = "Frontiers in Plant Science",
title = "Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae)",
volume = "14",
doi = "10.3389/fpls.2023.1211453"
}

Aničić, N., Matekalo, D., Skorić, M., Gašić, U. M., Nestorović Živković, J., Dmitrović, S., Božunović, J., Milutinović, M., Petrović, L., Dimitrijević, M., Anđelković, B. D.,& Mišić, D.. (2024). Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae). in Frontiers in Plant Science
Frontiers Media., 14.
https://doi.org/10.3389/fpls.2023.1211453

Aničić N, Matekalo D, Skorić M, Gašić UM, Nestorović Živković J, Dmitrović S, Božunović J, Milutinović M, Petrović L, Dimitrijević M, Anđelković BD, Mišić D. Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae). in Frontiers in Plant Science. 2024;14.
doi:10.3389/fpls.2023.1211453 .

Aničić, Neda, Matekalo, Dragana, Skorić, Marijana, Gašić, Uroš M., Nestorović Živković, Jasmina, Dmitrović, Slavica, Božunović, Jelena, Milutinović, Milica, Petrović, Luka, Dimitrijević, Milena, Anđelković, Boban D., Mišić, Danijela, "Functional iridoid synthases from iridoid producing and non-producing Nepeta species (subfam. Nepetoidae, fam. Lamiaceae)" in Frontiers in Plant Science, 14 (2024),
https://doi.org/10.3389/fpls.2023.1211453 . .