Functional characterization of a plastidal cation-dependent O-methyltransferase from the liverwort Plagiochasma appendiculatum

Xu, Rui-Xue; Zhou, Yu; Gao, Shuai; Zhang, Yuying; Li, Dandan; Lou, Hongxiang; Cheng, Ai‐Xia

doi:10.1016/j.phytochem.2015.08.002

Cited by 13 publications

(10 citation statements)

References 36 publications

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“…Enzymes such as anthocyanidin synthase and chalcone synthase in the flavonoid biosynthetic pathway were found in chloroplasts (Tian, Wan, Pan, Zheng, & Huang, ; Wang et al, ; Wang et al, ). The methylation of flavonoids occurs in chloroplasts in liverworts (Xu et al, ). This plastid and cytoplasm localization of SQD2.1 indicates that flavonoid glycosylation by SQD2.1 also occurs in chloroplasts and cytoplasm.…”

Section: Discussionmentioning

confidence: 99%

Rice sulfoquinovosyltransferase SQD2.1 mediates flavonoid glycosylation and enhances tolerance to osmotic stress

Zhan

Shen

Chen

et al. 2019

Plant Cell & Environment

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Sulfoquinovosyltransferase 2 (SQD2) catalyses the final step in the sulfoquinovosyldiacylglycerol (SQDG) biosynthetic pathway. It is involved in the phosphate starvation response. Here, we show that rice SQD2.1 has dual activities catalysing SQDG synthesis and flavonoid glycosylation. SQD2.1 null mutants (sqd2.1) in rice had decreased levels of glycosidic flavonoids, particularly apigenin 7‐O‐glucoside (A7G), whereas these metabolites were increased in rice plants overexpressing SQD2.1. The sqd2.1 mutants and SQD2.1 overexpressing lines showed reduced and enhanced, respectively, tolerance to salinity and drought. Treating the sqd2.1 mutants with A7G decreased oxidative damage and restored stress tolerance to the wild‐type levels. These findings demonstrate that SQD2.1 has a novel function in the glycosylation of flavonoids that is required for osmotic stress tolerance in rice. The novel activity of SQD2.1 in the production of glycosidic flavonoids improves scavenging of reactive oxygen species and protects against excessive oxidation.

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Section: Discussionmentioning

confidence: 99%

Rice sulfoquinovosyltransferase SQD2.1 mediates flavonoid glycosylation and enhances tolerance to osmotic stress

Zhan

Shen

Chen

et al. 2019

Plant Cell & Environment

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“…The CCoAOMT and CCoAOMT-like proteins phylogeny together with the specificity of gene structures within the clades, suggest that cyanobacterial genes from clade 2 are ancestors of all CCoAOMT and CCoAOMT-like genes. The presence of the genes from clades 1a and 2 in the Physcomitrella patens genome and the identification of clade 1a gene in liverwort P. appendiculatum suggest that superclade 1 arose at the very early stage of land plant evolution (Xu et al 2015 ). During manuscript preparation, the Marchantia polymorpha genome sequence was released (Bowman et al 2017 ).…”

Section: Discussionmentioning

confidence: 99%

Sorghum CCoAOMT and CCoAOMT-like gene evolution, structure, expression and the role of conserved amino acids in protein activity

et al. 2018

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Sorghum is a crop plant that is grown for seeds, sucrose, forage and biofuel production. In all these applications, lignin is a superfluous component that decreases the efficiency of technological processes. Caffeoyl-coenzyme A O-methyltransferase (CCoAOMT) is an enzyme involved in monolignol synthesis that affects the efficiency of lignification and lignin composition. The sorghum genome harbors one CCoAOMT gene and six closely related CCoAOMT-like genes. The structures of four sorghum CCoAOMT-like enzymes suggest that these proteins might methylate caffeoyl coenzyme A and contribute to monolignol synthesis. In this study, two sorghum genes, CCoAOMT and one CCoAOMT-like, were found to be highly expressed in leaves, stems and immature seeds. The promoters of these genes possess clusters of transcription factor-binding sites specific for lignification, and this suggests that they are important for lignification. Phylogenetic analysis revealed that one sorghum CCoAOMT-like enzyme is closely related to ancestral cyanobacterial CCoAOMT-like proteins. The remaining CCoAOMT-like enzymes, including the one highly expressed in the leaves and stem, are closely related to CCoAOMT. Genes from these two groups possess different, evolutionarily conserved gene structures. The structure of the sorghum CCoAOMT-like protein from the ancestral clade was modeled and differences between enzymes from the two clades were analyzed. These results facilitate a better understanding of the evolution of genes involved in lignification, and provide valuable data for sorghum improvement through traditional breeding or molecular genetic techniques. The findings suggest that CCoAOMT-like genes might be recruited in lignification and raise questions of the frequency of such functional shifts.Electronic supplementary materialThe online version of this article (10.1007/s00438-018-1441-6) contains supplementary material, which is available to authorized users.

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“…). However, PaOMT1 from P. appendiculatum has been reported directing to the chloroplast . It may attribute to the differences in their enzyme features.…”

Section: Resultsmentioning

confidence: 96%

“…Sequence alignment also revealed differences with respect to both the metal‐ and SAM‐binding sites: only two of the six substrate‐binding sites present in M. sativa CCoAOMT were retained in PaF6OMT. The level of similarity between PaF6OMT and PaOMT1 (KP729179), the first O ‐methyltransferase characterized in a liverwort , was also low (16.2%). However, the sequence matched more closely with both R. norvegicus CatOMT (1JR4‐A) (33.5%) and N. concave CatOMT (WP‐051178395.1) (45.2%).…”

Section: Resultsmentioning

confidence: 98%

“…The reaction products of quercetin and luteolin were identified by HPLC separation using the corresponding 3′‐ O ‐methylether (isorhamnetin and chrysoeriol) as the product standards. Eriodictyol was accepted as substrate and generated an unusual para‐methylated product due to the existence of chiral carbon on its C‐ring . PaF6OMT can also accept esculetin, caffeoyl CoA, and caffeoyl alcohol as substrates, converting them to scopoletin, feruloyl CoA, coniferyl alcohol, respectively, as identified by chromatography with the corresponding authentic standard.…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

Enzymatic production of oroxylin A and hispidulin using a liverwort flavone 6‐O‐methyltransferase

Zhang

Gao

et al. 2016

FEBS Letters

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Edited by Richard CogdellOroxylin A and hispidulin, compounds which are abundant in both Scutellaria and liverwort species, are important lead compounds for the treatment of ischemic cerebrovascular disease. Their enzymatic synthesis requires an Omethyltransferase able to interact with the related flavonoid's 6-OH group, but such an enzyme has yet to be identified in plants. Here, the gene encoding an O-methyltransferase (designated PaF6OMT) was isolated from the liverwort species Plagiochasma appendiculatum. A test of alternative substrates revealed that its strongest preferences were baicalein and scutellarein, which were converted into, respectively, oroxylin A and hispidulin. Allowed a sufficient reaction time, the conversion rate of these two substrates was, respectively, 90% and 100%. PaF6OMT offers an enzymatic route to the synthesis of oroxylin A and hispidulin.

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Functional characterization of a plastidal cation-dependent O-methyltransferase from the liverwort Plagiochasma appendiculatum

Cited by 13 publications

References 36 publications

Rice sulfoquinovosyltransferase SQD2.1 mediates flavonoid glycosylation and enhances tolerance to osmotic stress

Rice sulfoquinovosyltransferase SQD2.1 mediates flavonoid glycosylation and enhances tolerance to osmotic stress

Sorghum CCoAOMT and CCoAOMT-like gene evolution, structure, expression and the role of conserved amino acids in protein activity

Enzymatic production of oroxylin A and hispidulin using a liverwort flavone 6‐O‐methyltransferase

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