A Novel Polyamine Acyltransferase Responsible for the Accumulation of Spermidine Conjugates in <i>Arabidopsis</i> Seed

Luo, Jie; Fuell, Christine; Parr, Adrian; Hill, Lionel; Bailey, Paul; Elliott, Katherine A.; Fairhurst, Shirley A.; Martin, Cathie; Michael, Anthony J.

doi:10.1105/tpc.108.063511

Cited by 148 publications

(142 citation statements)

References 67 publications

(85 reference statements)

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“…As an initial step to understand the genetic determinants of PAs, we focused on the possible role of acylation, the final and key step in PA biosynthesis, by looking for BAHD acyltransferases within the confidence intervals of the identified loci (Grienenberger et al, 2009;Luo et al, 2009;Onkokesung et al, 2012;Wen et al, 2014). Eleven candidate genes that were made up of five tandem pairs were assigned to the loci identified, with two of them having been partially characterized in a previous study (Figures 3 and 4B;Chen et al, 2014).…”

Section: Assignment Of Candidate Genes In the Bahd Acyltransferase Famentioning

confidence: 99%

“…Phylogenetic relationships among the BAHD acyltransferases were then investigated by reconstructing the phylogenetic tree ( Figure 4A), using a neighbor-joining algorithm, based on the amino acid sequences of our candidates and a collection of 27 reported plant BAHD acyltransferases (D'Auria, 2006;Grienenberger et al, 2009;Luo et al, 2009;Onkokesung et al, 2012;Chen et al, 2014;Dong et al, 2015). The resulting phylogenetic tree is consistent with that of Tuominen et al (2011), an updated version of that from D'Auria, who sorted biochemically characterized BAHD acyltransferases into eight major clades (A) An unrooted phylogenetic tree was constructed as described in Methods.…”

Section: Assignment Of Candidate Genes In the Bahd Acyltransferase Famentioning

confidence: 99%

“…ACTs (agmatine coumaroyl transferases) were characterized in barley and in Arabidopsis thaliana (Burhenne et al, 2003;Muroi et al, 2009). Spermidine hydroxycinnamoyl transferases responsible for the production of hydroxycinnamoyl spermidines have been identified in Arabidopsis, Nicotiana attenuata, and rice (Grienenberger et al, 2009;Luo et al, 2009;Onkokesung et al, 2012;Dong et al, 2015). More recently, PHTs (putrescine hydroxycinnamoyl transferases) have been identified in both dicots (Nicotiana) and monocots such as maize and rice (Onkokesung et al, 2012;Wen et al, 2014;Chen et al, 2014).…”

Section: Introductionmentioning

confidence: 99%

“…To date, the identification of hydroxycinnamoyl transferases has been achieved mostly by reverse genetics (Suzuki et al, 2002;Lepelley et al, 2007;Grienenberger et al, 2009;Luo et al, 2009;Elejalde-Palmett et al, 2015), and the role of these enzymes in determining the natural variation of PAs remains to be investigated. The combination of high-throughput metabolic profiling with large-scale genome resequencing by Structures of benzoyl-CoA and hydroxycinnamoyl-CoAs are shown as R1 to R5.…”

Section: Introductionmentioning

confidence: 99%

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Evolutionarily Distinct BAHD N-acyltransferases are Responsible for Natural Variation of Aromatic Amine Conjugates in Rice

et al. 2016

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Phenolamides (PAs) are specialized (secondary) metabolites mainly synthesized by BAHD N-acyltransferases. Here, we report metabolic profiling coupled with association and linkage mapping of 11 PAs in rice (Oryza sativa). We identified 22 loci affecting PAs in leaves and 16 loci affecting PAs in seeds. We identified eight BAHD N-acyltransferases located on five chromosomes with diverse specificities, including four aromatic amine N-acyltransferases. We show that genetic variation in PAs is determined, at least in part, by allelic variation in the tissue specificity of expression of the BAHD genes responsible for their biosynthesis. Tryptamine hydroxycinnamoyl transferase 1/2 (Os-THT1/2) and tryptamine benzoyl transferase 1/2 (Os-TBT1/2) were found to be bifunctional tryptamine/tyramine N-acyltransferases. The specificity of Os-THT1 and Os-TBT1 for agmatine involved four tandem arginine residues, which have not been identified as specificity determinants for other plant BAHD transferases, illustrating the versatility of plant BAHD transferases in acquiring new acyl acceptor specificities. With phylogenetic analysis, we identified both divergent and convergent evolution of N-acyltransferases in plants, and we suggest that the BAHD family of tryptamine/tyramine N-acyltransferases evolved conservatively in monocots, especially in Gramineae. Our work demonstrates that omics-assisted gene-to-metabolite analysis provides a useful tool for bulk gene identification and crop genetic improvement.

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Section: Assignment Of Candidate Genes In the Bahd Acyltransferase Famentioning

confidence: 99%

Section: Assignment Of Candidate Genes In the Bahd Acyltransferase Famentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Evolutionarily Distinct BAHD N-acyltransferases are Responsible for Natural Variation of Aromatic Amine Conjugates in Rice

et al. 2016

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“…Acylation of natural products contributes to structural and functional diversity and has in addition been linked to the chemical stability of a number of compounds. The best-studied family of plant natural product acyltransferases is the BAHD family, the members of which are collectively responsible for acylation of a wide range of compounds (Yang et al, 1997;Dudareva et al, 1998;Fujiwara et al, 1998;St Pierre et al, 1998;Walker et al, 2002;Luo et al, 2007Luo et al, , 2009; Grienenberger et al, 2009). Members of the BAHD family are involved in the synthesis of important natural products, including the anticancer drugs vinblastine (St Pierre et al, 1998) and taxol (Kingston 1994;Walker et al, 2002).…”

Section: Introductionmentioning

confidence: 99%

A Serine Carboxypeptidase-Like Acyltransferase Is Required for Synthesis of Antimicrobial Compounds and Disease Resistance in Oats

et al. 2009

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Serine carboxypeptidase-like (SCPL) proteins have recently emerged as a new group of plant acyltransferases. These enzymes share homology with peptidases but lack protease activity and instead are able to acylate natural products. Several SCPL acyltransferases have been characterized to date from dicots, including an enzyme required for the synthesis of glucose polyesters that may contribute to insect resistance in wild tomato (Solanum pennellii) and enzymes required for the synthesis of sinapate esters associated with UV protection in Arabidopsis thaliana. In our earlier genetic analysis, we identified the Saponin-deficient 7 (Sad7) locus as being required for the synthesis of antimicrobial triterpene glycosides (avenacins) and for broad-spectrum disease resistance in diploid oat (Avena strigosa). Here, we report on the cloning of Sad7 and show that this gene encodes a functional SCPL acyltransferase, SCPL1, that is able to catalyze the synthesis of both N-methyl anthraniloyl-and benzoyl-derivatized forms of avenacin. Sad7 forms part of an operon-like gene cluster for avenacin synthesis. Oat SCPL1 (SAD7) is the founder member of a subfamily of monocot-specific SCPL proteins that includes predicted proteins from rice (Oryza sativa) and other grasses with potential roles in secondary metabolism and plant defense.

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Phenylpropanoid Metabolism

Rock

2017

Encyclopedia of Life Sciences

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Phenylpropanoid compounds encompass a wide range of structural classes with diverse biological functions in defence, survival and structural support associated with normal plant development (belying the term 'secondary metabolite'). The biosynthesis of phenylpropanoids is regulated by diverse environmental stimuli. Phenylpropanoid metabolism (other than flavonoids, not covered here) occupies a central place in the general aromatic metabolism of plants from shikimate to phenylalanine to lignin polymers and also to coumarins, phenolic volatiles and hydrolysable tannins. In recent years, genetics and biochemistry, along with methodology‐driven, computational, transgenic and comparative transcriptomic approaches, have led to significant advances in the identification of the families of genes encoding enzymes, transporters, regulatory factors involved in phenylpropanoid metabolism and a clearer picture of their functions in biotic and abiotic stress responses, plant development and enzyme/pathway evolution driven by interactions of species with their environment. Key Concepts Having one phenyl aromatic ring with one or more hydroxyl groups attached gives phenylpropanoids amphiphilic and reducing properties, underlying their ability to physically interact with other biomolecules. Plants invest a large percentage of their fixed carbon into synthesising phenylpropanoids, from simple volatile phenolic acids such as the defence hormone salicylic acid to complex polyphenolic flavonoids encompassing thousands of compounds with myriad physiological and adaptive functions. The shikimate pathway is the starting point for phenylpropanoid biosynthesis from shikimate product phenylalanine ( l ‐Phe), via the intermediate chorismate, which also serves as substrate for the synthesis of quinones and tocopherols important as electron acceptors in photosynthesis and aerobic respiration. Phenylpropanoid biosynthesis proceeds from deamination of Phe to cinnamate by the rate‐limiting and environmentally regulated enzyme PAL, followed by oxidation of the ring to p ‐coumarate, its activation with coenzymeA and a series of hydroxylation, methylation and reduction reactions to give cinnamic acids, ‐aldehydes and ‐alcohols that serve as substrates to generate a wide range of complex structures, notably polymers of coumaroyl, conferyl and sinapyl alcohols comprising lignin. Recent studies have established the major pathway in plants which proceeds from p ‐coumaroyl‐CoA → p ‐coumaryl‐shikimate → caffeoyl‐shikimate → caffeoyl‐CoA → feruloyl CoA → coniferaldehyde → 5‐OH coniferaldehyde → sinapaldehyde → sinapate/sinapyl alcohol (oxidation versus reduction, respectively), instead of the original model of a grid/matrix of parallel ring oxidation and side‐chain redox pathways from hydroxycinnamic acids to alcohols. Synthesis involves three subcellular compartments: chloroplast for Phe, cytosol for sinapoyl‐esters and the vacuole for trans‐esterifications. The identity of specific transporters, temporal‐ or organ‐specific regulatory factors for phenylpropanoid flux to (in)soluble polymers in the apoplast in response to biotic and abiotic stressors and whether lignin formation proceeds via precise channeling of individual precursors through metabolons (temporary structural–functional complexes formed between sequential enzymes) are key questions of practical significance that remain to be answered.

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A Novel Polyamine Acyltransferase Responsible for the Accumulation of Spermidine Conjugates in Arabidopsis Seed

Cited by 148 publications

References 67 publications

Evolutionarily Distinct BAHD N-acyltransferases are Responsible for Natural Variation of Aromatic Amine Conjugates in Rice

Evolutionarily Distinct BAHD N-acyltransferases are Responsible for Natural Variation of Aromatic Amine Conjugates in Rice

A Serine Carboxypeptidase-Like Acyltransferase Is Required for Synthesis of Antimicrobial Compounds and Disease Resistance in Oats

Phenylpropanoid Metabolism

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