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OsCAldOMT1 is a bifunctional O-methyltransferase involved in the biosynthesis of tricin-lignins in rice cell walls.

ABSTRACT: Lignin is a phenylpropanoid polymer produced in the secondary cell walls of vascular plants. Although most eudicot and gymnosperm species generate lignins solely via polymerization of p-hydroxycinnamyl alcohols (monolignols), grasses additionally use a flavone, tricin, as a natural lignin monomer to generate tricin-incorporated lignin polymers in cell walls. We previously found that disruption of a rice 5-HYDROXYCONIFERALDEHYDE O-METHYLTRANSFERASE (OsCAldOMT1) reduced extractable tricin-type metabolites in rice vegetative tissues. This same enzyme has also been implicated in the biosynthesis of sinapyl alcohol, a monolignol that constitutes syringyl lignin polymer units. Here, we further demonstrate through in-depth cell wall structural analyses that OsCAldOMT1-deficient rice plants produce altered lignins largely depleted in both syringyl and tricin units. We also show that recombinant OsCAldOMT1 displayed comparable substrate specificities towards both 5-hydroxyconiferaldehyde and selgin intermediates in the monolignol and tricin biosynthetic pathways, respectively. These data establish OsCAldOMT1 as a bifunctional O-methyltransferase predominantly involved in the two parallel metabolic pathways both dedicated to the biosynthesis of tricin-lignins in rice cell walls. Given that cell wall digestibility was greatly enhanced in the OsCAldOMT1-deficient rice plants, genetic manipulation of CAldOMTs conserved in grasses may serve as a potent strategy to improve biorefinery applications of grass biomass.

SUBMITTER: Lam PY

PROVIDER: S-EPMC6690965 | biostudies-literature | 2019 Aug

REPOSITORIES: biostudies-literature

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OsCAldOMT1 is a bifunctional O-methyltransferase involved in the biosynthesis of tricin-lignins in rice cell walls.

Lam Pui Ying PY Tobimatsu Yuki Y Matsumoto Naoyuki N Suzuki Shiro S Lan Wu W Takeda Yuri Y Yamamura Masaomi M Sakamoto Masahiro M Ralph John J Lo Clive C Umezawa Toshiaki T

Scientific reports 20190812 1

Lignin is a phenylpropanoid polymer produced in the secondary cell walls of vascular plants. Although most eudicot and gymnosperm species generate lignins solely via polymerization of p-hydroxycinnamyl alcohols (monolignols), grasses additionally use a flavone, tricin, as a natural lignin monomer to generate tricin-incorporated lignin polymers in cell walls. We previously found that disruption of a rice 5-HYDROXYCONIFERALDEHYDE O-METHYLTRANSFERASE (OsCAldOMT1) reduced extractable tricin-type met ...[more]

PMID: 31406182

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Project description:Salt stress limits plant growth and agricultural productivity and plants have evolved suitable mechanisms to adapt to salinity environments. It is important to characterize genes involved in plant salt tolerance, which will advance our understanding of mechanisms mediating salt tolerance and help researchers design ways to improve crop performances under high salinity environments. Here, we reported a CYP450 family member, CYP75B4, improves salt tolerance of rice seedlings by inducing flavonoid tricin and cell wall lignin accumulation. The CYP75B4 is highly expressed in tissues rich in cell walls and induced by salt treatment. Subcellular localization analysis revealed that CYP75B4 is localized in the endoplasmic reticulum (ER). The CYP75B4 overexpressing (CYP75B4-OE) lines showed significant enhancement in stem mechanical strength, whereas the cyp75b4 null mutants displayed weaker stems, as compared to the wild-type. Notably, the cyp75b4 and CYP75B4-OE lines showed decreased and improved, respectively, salt tolerance performances in terms of survival rate, ROS accumulation, and Na+/ K+ homeostasis. Additionally, the cyp75b4 mutants had a decreased tricin level, whereas CYP75B4-OE lines showed an increased tricin content, under both control or salinity conditions. Furthermore, treating the cyp75b4 mutants with tricin partly resorted salt stress tolerance to the wild-type levels, indicating a role of CYP75B4-mediated tricin production in rice response to salinity. Consistently, another tricin-deficient mutant cyp93g1 also displayed salt sensitivity and the tricin application could partly restore its salt-sensitive phenotypes. Moreover, the CYP75B4 significantly promotes lignin deposition in cell walls of mature stems and seedlings under salinity conditions, which probably contributes to the enhanced stem mechanical strength and improved salt tolerance in CYP75B4-OE plants. Our findings reveal a novel function of CYP75B4 in rice salt tolerance and lodging resistance by inducing tricin accumulation and lignin deposition in cell walls.

Project description:BackgroundSecondary metabolites biosynthesized by polyketide synthase (PKS) and nonribosomal peptide synthetase (NRPS) family of enzymes constitute several classes of therapeutically important natural products like erythromycin, rapamycin, cyclosporine etc. In view of their relevance for natural product based drug discovery, identification of novel secondary metabolite natural products by genome mining has been an area of active research. A number of different tailoring enzymes catalyze a variety of chemical modifications to the polyketide or nonribosomal peptide backbone of these secondary metabolites to enhance their structural diversity. Therefore, development of powerful bioinformatics methods for identification of these tailoring enzymes and assignment of their substrate specificity is crucial for deciphering novel secondary metabolites by genome mining.ResultsIn this work, we have carried out a comprehensive bioinformatics analysis of methyltransferase (MT) domains present in multi functional type I PKS and NRPS proteins encoded by PKS/NRPS gene clusters having known secondary metabolite products. Based on the results of this analysis, we have developed a novel knowledge based computational approach for detecting MT domains present in PKS and NRPS megasynthases, delineating their correct boundaries and classifying them as N-MT, C-MT and O-MT using profile HMMs. Analysis of proteins in nr database of NCBI using these class specific profiles has revealed several interesting examples, namely, C-MT domains in NRPS modules, N-MT domains with significant homology to C-MT proteins, and presence of NRPS/PKS MTs in association with other catalytic domains. Our analysis of the chemical structures of the secondary metabolites and their site of methylation suggested that a possible evolutionary basis for the presence of a novel class of N-MT domains with significant homology to C-MT proteins could be the close resemblance of the chemical structures of the acceptor substrates, as in the case of pyochelin and yersiniabactin. These two classes of MTs recognize similar acceptor substrates, but transfer methyl groups to N and C positions on these substrates.ConclusionWe have developed a novel knowledge based computational approach for identifying MT domains present in type I PKS and NRPS multifunctional enzymes and predicting their site of methylation. Analysis of nr database using this approach has revealed presence of several novel MT domains. Our analysis has also given interesting insight into the evolutionary basis of the novel substrate specificities of these MT proteins.

Dataset Information

OsCAldOMT1 is a bifunctional O-methyltransferase involved in the biosynthesis of tricin-lignins in rice cell walls.

Publications

OsCAldOMT1 is a bifunctional O-methyltransferase involved in the biosynthesis of tricin-lignins in rice cell walls.

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