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PubMed2025

The Tartary Buckwheat FtMYB46-FtNRAMP3 Module Enhances Plant Lead and Cadmium Tolerance.

The presence of toxic heavy metals lead (Pb) and cadmium (Cd) in polluted soil damage crop production and consequently harms human and livestock health. Tartary buckwheat (Fagopyrum tataricum) is a potential model plant for heavy metal phytoremediation because of its valuable characteristics of high heavy metal tolerance and abundant biomass production. Here, we report that the Tartary buckwheat FtMYB46-FtNRAMP3 module enhances plant Pb and Cd tolerance. RNA sequencing analysis showed that Pb treatment specifically induced expression of FtNRAMP3, a member of the NRAMP (Natural Resistance-Associated Macrophage Protein) transporter gene family. Further cytological and biochemical analysis revealed that FtNRAMP3 was localised to the plasma membrane and significantly contributed to increased tolerance to Pb and Cd in yeast cells. Consistently, transgenic overexpression of FtNRAMP3 in Arabidopsis significantly increased plant tolerance to Pb and Cd applications, reducing Pb concentration but increasing Cd concentration in the overexpression transgenic plants. Subsequent yeast one-hybrid and electrophoretic mobility shift assays showed that the transcription factor FtMYB46 directly binds to the FtNRAMP3 promoter. Further, FtMYB46 promoted FtNRAMP3 expression and increased plant Pb and Cd tolerance. Overall, this study demonstrates the important role of the FtMYB46-FtNRAMP3 module and its potential value in the phytoremediation of Pb and Cd stress.

Cadmium↗

PubMed2025

Comparative analysis of DREB gene family in buckwheat: the role of FtDREB02 in the delphinidin biosynthesis and drought stress response.

Dehydration response element binding (DREB) transcription factors play a pivotal role in plant abiotic stress responses, but its evolutionary and functional characterization in buckwheat remains unexplored. Here, we conducted a comprehensive analysis of the DREB gene family across three buckwheat species, revealing segmental duplication as the primary driver of family expansion and potential purifying selection during evolution. A FtDREB02 gene, classified as group A2, was identified through genome-wide association analysis (GWAS) on drought tolerance and delphinidin content. Functional validation in Arabidopsis thaliana and the hairy root of Tartary buckwheat (Fagopyrum tataricum) demonstrated that overexpression of this gene promotes delphinidin biosynthesis and enhances plant resistance to water scarcity. Through the integration of DAP-seq and PEG transcriptome cluster analysis, a FtANS candidate was screened. Functional studies showed that FtDREB02 regulates delphinidin content by binding directly to DRE elements of the FtANS promoter. This research identifies and comprehensively analyzes the DREB family within buckwheat species, elucidating the regulatory mechanisms of FtDREB02 in controlling flavonoid biosynthesis and drought resistance, providing potential genetic resources for breeding buckwheat varieties with excellent agronomic traits.

Anthocyanins↗

PubMed2025

In silico, in vitro, and in vivo characterization of thiamin-binding proteins from plant seeds.

Thiamin, an essential micronutrient, is a cofactor for enzymes involved in the central carbon metabolism and amino acid pathways. Despite efforts to enhance thiamin content in rice by incorporating thiamin biosynthetic genes, increasing thiamin content in the endosperm remains challenging, possibly due to a lack of thiamin stability and/or a local sink. The introduction of storage proteins has been successful in several biofortification strategies, and similar efforts targeting thiamin have been performed, leading to a 3-4-fold increase in white rice. However, only one thiamin-binding protein (TBP) sequence has been described in plants, more specifically from sesame seeds. Therefore, we aimed to identify and characterize TBPs, as well as to evaluate the effect of their expression on thiamin concentration, using a comprehensive approach integrating in silico, in vitro, and in vivo methods. We identified the sequences of putative TBPs from Oryza sativa (Os, rice), Fagopyrum esculentum (Fe, buckwheat), and Zea mays (Zm, maize) and pinpointed the thiamin-binding pockets through molecular docking. FeTBP and OsTBP contained one pocket with binding affinities similar to the Escherichia coli TBP, a well-characterized TBP, supporting their function as TBPs. In vivo expression studies of TBPs in tobacco leaves and rice callus resulted in increased thiamin levels, with FeTBP and OsTBP showing the most pronounced effects. Additionally, thermal shift assays confirmed the thiamin-binding capabilities of FeTBP and OsTBP, as observed by the significant increases in melting temperatures upon thiamin binding, indicating protein stabilization. These findings offer new insights into the diversity and function of plant TBPs and highlight the potential of FeTBP and OsTBP to modulate thiamin levels in crop plants.

Thiamine↗

PubMed1978

[Detection and distribution of "rutinase+, an enzyme hydrolyzin; rutoside].

125 species were investigated for rutinase. A high enzyme activity was found only in a few genera: Fagopyrum, Rhamnus, Berchemia, Sophora, Datisca and Danae. Lower activity was detected in several Lichens (Parmeliaceae) and diverse plants but is lacking in some specimens. In a number of species containing 3- or 7-rutinosides, no enzyme able to hydrolyse the latter seems to be present.

Fungi↗

PubMed1977

[Benzoyl-DL-arginine-p-nitroanilidase from buckwheat seeds. Properties and substrate specificity].

A proteolytic enzyme, hydrolyzing N-benzoyl-D,L-arginine-p-nitro-anilide (BAPAase), has been isolated from the buckwheat seeds (Fagopyrum esculentum). The enzyme was purified 400-fold and was homogeneous according to isoelectrofocusing and disc electrophoresis in polyacrylamide gel. The molecular weight of the BAPAase was determined to be 65000 by gel-chromatography and 70000 by polyacrylamide gel electrophoresis. The sedimentation coefficient of the BAPAase was found to be 4.3 S, the isoelectric point--pH 4.5. The enzyme split peptide, esteric and amide bonds formed by carboxyl groups of lysine and arginine in synthetic substrates. The enzyme did not hydrolyse fibrinogen, did not activate chimotrypsinogen, weakly hydrolyzed histones and casein and strongly--protamine. The BAPAase did not hydrolyse albumins and globulins from the buckwheat seeds, and weakly hydrolyzed glutelins. The study of the products of the hydrolysis of salmine and sturine by BAPAase showed that the enzyme split internal peptide bonds in these substrates, and, thus, it is an endopeptidase.

Benzoylarginine Nitroanilide↗