Prenyltransferases catalyzing geranyldiphosphate formation in tomato fruit

Hivert, Gal; Davidovich‐Rikanati, Rachel; Bar, Einat; Sitrit, Yaron; Schaffer, Arthur A.; Dudareva, Natalia; Lewinsohn, Efraim

doi:10.1016/j.plantsci.2020.110504

Cited by 16 publications

(7 citation statements)

References 46 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This Genevestigator differential expression profile might be a consequence of different genetic backgrounds used in the experiments. In agreement with this hypothesis, SSU-I transcript levels are very low in cultivated tomatoes (S. lycopersicum) but are abundant in the fruits of wild relatives (S. pimpinellifolium and S. cheesmaniae), which produce substantially more monoterpenes (Hivert et al, 2020). Whereas MicroTom has been broadly used for infection experiments with some bacteria and fungi (Costa et al, 2021;Deganello et al, 2014;Nakahara et al, 2016), previous experiments using Pst found no wilt symptoms or bacterial growth eight days after infection (Takahashi et al, 2005), strongly suggesting that Pst is just an opportunistic MicroTom pathogen.…”

Section: Slg1 Is Not Required For Monoterpene Synthesis In Leavessupporting

confidence: 59%

“…Similar to SlG1 , tomato NDPS1 , GPPS and SSU-I genes are induced in Pst -infected leaves, with SlG1, SSU-I and NDPS1 showing the strongest upregulation (Figure S4). SlG1/SSU-I heterodimers have been shown to mainly produce GPP in vitro (Zhou & Pichersky, 2020) and SlG2/SSU-I heterodimers have been found to produce GPP for monoterpene biosynthesis in tomato fruit (Hivert et al, 2020). Based on these data, we hypothesized that SlG1 might participate in the production of monoterpenes in leaves.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Tomato geranylgeranyl diphosphate synthase isoform 1 specifically interacts with phytoene synthase isoform 3 to produce strigolactones in tomato roots

Ezquerro¹,

Barja³

et al. 2022

Preprint

View full text Add to dashboard Cite

Carotenoids are photoprotectant pigments and precursors of the hormones abscisic acid (ABA) and strigolactones (SL). Carotenoids are produced in plastids from geranylgeranyl diphosphate (GGPP), which is diverted to the carotenoid pathway by phytoene synthase (PSY). In tomato (Solanum lycopersicum), 3 genes encode plastid-targeted GGPP synthases (SlG1 to 3) and 3 genes encode PSY isoforms (PSY1 to 3). Here we investigated the function of SlG1 by generating loss-of-function lines and combining their metabolic and physiological phenotypes with gene co-expression and co-immunoprecipitation analyses. Leaves and fruits of slg1 lines showed a wild-type phenotype in terms of isoprenoid accumulation, photosynthesis and development. Consistently, SlG1 is co-expressed with PSY3 and other genes involved in the production of carotenoids and SL (but not ABA) only in roots. SlG1 was also found to physically interact with the root-specific PSY3 isoform (and not with PSY1 and PSY2). Root SL (but not ABA) levels were reduced in slg1 lines. Our results confirm a specific role of SlG1 in SL production in combination with PSY3. This role appears to be restricted to roots as slg1 plants do not exhibit the shoot phenotype displayed by other SL-deficient mutants.

show abstract

Section: Slg1 Is Not Required For Monoterpene Synthesis In Leavessupporting

confidence: 59%

Section: Resultsmentioning

confidence: 99%

Tomato geranylgeranyl diphosphate synthase isoform 1 specifically interacts with phytoene synthase isoform 3 to produce strigolactones in tomato roots

Ezquerro¹,

Barja³

et al. 2022

Preprint

View full text Add to dashboard Cite

show abstract

“…Prenyltransferases constitute a large family of enzymes, synthesizing a variety of isoprenoids (Akhtar et al, 2013; Chen et al, 1994; Hivert et al, 2020; Liang et al, 2002; Tholl, 2015). Short‐chain prenyltransferases in the isoprenoid biosynthesis pathway include geranyl diphosphate synthase (GPPS), farnesyl diphosphate synthase (FPPS) and geranylgeranyl diphosphate synthase (GGPPS).…”

Section: Introductionmentioning

confidence: 99%

Farnesyl/geranylgeranyl diphosphate synthases regulate the biosynthesis of alarm pheromone in a unique manner in the vetch aphid Megoura viciae

Song

Qin

Zhang

et al. 2022

Insect Molecular Biology

View full text Add to dashboard Cite

Farnesyl/geranylgeranyl diphosphate synthases (FPPS/GGPPS) as the short‐chain prenyltransferases catalyse the formation of the acyclic precursors (E)‐FPP and (E)‐GGPP for isoprenoid biosynthesis. Here, we first cloned the cDNAs encoding FPPS and GGPPS in the vetch aphid Megoura viciae (designated as MvFPPS and MvGGPPS). They had an open reading frame of 1185 and 930 bp in length, encoding 395 and 309 amino acids, with a theoretical isoelectric point of 6.52 and 6.21, respectively. Sequence alignment and phylogenetic analysis showed that MvFPPS and MvGGPPS shared the conserved aspartate‐rich motifs characterized by all prenyltransferases identified to date and were clustered with their homologues in two large clades. RNA interference (RNAi) combined with gas chromatography/mass spectrometry (GC–MS) analysis showed that both MvFPPS and MvGGPPS were involved in the biosynthesis of alarm pheromone. Spatiotemporal expression profiling showed that the expression of MvFPPS and MvGGPPS was significantly higher in embryos than in other tissues. RNAi and GC–MS performed specifically in embryos corroborated the function of MvFPPS and MvGGPPS. In vitro, enzymatic activity assay and product analysis demonstrated that MvFPPS could catalysed the formation of (E)‐FPP using DMAPP or (E)‐GPP as the allylic cosubstrates in the presence of IPP, while MvGGPPS could only use (E)‐GPP or (E)‐FPP as cosubstrates. Functional interaction analysis using RNAi revealed that MvGGPPS exerts unidirectional functional compensation for MvFPPS. Moreover, it can regulate the biosynthesis of alarm pheromone by imposing a negative feedback regulation on MvFPPS. Our study helps to understand the molecular regulatory mechanism of terpenoid biosynthesis in the aphid.

show abstract

“…IPP and DMAPP can be condensed (head to tail) by prenyltransferase (PTS) or isoprenyl diphosphate synthase (IDS), resulting in a series of prenyl diphosphates with various chain lengths. These linear precursors are then catalyzed by terpene synthase (TPS) and other modifying enzymes to form a variety of different terpenoids ( Tholl and Lee, 2011 ; Athanasakoglou and Grypioti, 2019 ; Johnson et al, 2019 ; Johnson and Bhat, 2019 ; Adal and Mahmoud, 2020 ; Hivert et al, 2020 ; Miller and Bhat, 2020 ).…”

Section: Introductionmentioning

confidence: 99%

Genome-Wide Identification and Functional Characterization of the Trans-Isopentenyl Diphosphate Synthases Gene Family in Cinnamomum camphora

et al. 2021

View full text Add to dashboard Cite

Trans-isopentenyl diphosphate synthases (TIDSs) genes are known to be important determinants for terpene diversity and the accumulation of terpenoids. The essential oil of Cinnamomum camphora, which is rich in monoterpenes, sesquiterpenes, and other aromatic compounds, has a wide range of pharmacological activities and has therefore attracted considerable interest. However, the TIDS gene family, and its relationship to the camphor tree (C. camphora L. Presl.), has not yet been characterized. In this study, we identified 10 TIDS genes in the genome of the C. camphora borneol chemotype that were unevenly distributed on chromosomes. Synteny analysis revealed that the TIDS gene family in this species likely expanded through segmental duplication events. Furthermore, cis-element analyses demonstrated that C. camphora TIDS (CcTIDS) genes can respond to multiple abiotic stresses. Finally, functional characterization of eight putative short-chain TIDS proteins revealed that CcTIDS3 and CcTIDS9 exhibit farnesyl diphosphate synthase (FPPS) activity, while CcTIDS1 and CcTIDS2 encode geranylgeranyl diphosphate synthases (GGPPS). Although, CcTIDS8 and CcTIDS10 were found to be catalytically inactive alone, they were able to bind to each other to form a heterodimeric functional geranyl diphosphate synthase (GPPS) in vitro, and this interaction was confirmed using a yeast two-hybrid assay. Furthermore, transcriptome analysis revealed that the CcTIDS3, CcTIDS8, CcTIDS9, and CcTIDS10 genes were found to be more active in C. camphora roots as compared to stems and leaves, which were verified by quantitative real-time PCR (qRT-PCR). These novel results provide a foundation for further exploration of the role of the TIDS gene family in camphor trees, and also provide a potential mechanism by which the production of camphor tree essential oil could be increased for pharmacological purposes through metabolic engineering.

show abstract

Prenyltransferases catalyzing geranyldiphosphate formation in tomato fruit

Cited by 16 publications

References 46 publications

Tomato geranylgeranyl diphosphate synthase isoform 1 specifically interacts with phytoene synthase isoform 3 to produce strigolactones in tomato roots

Tomato geranylgeranyl diphosphate synthase isoform 1 specifically interacts with phytoene synthase isoform 3 to produce strigolactones in tomato roots

Farnesyl/geranylgeranyl diphosphate synthases regulate the biosynthesis of alarm pheromone in a unique manner in the vetch aphid Megoura viciae

Genome-Wide Identification and Functional Characterization of the Trans-Isopentenyl Diphosphate Synthases Gene Family in Cinnamomum camphora

Contact Info

Product

Resources

About