OsEUL Lectin Gene Expression in Rice: Stress Regulation, Subcellular Localization and Tissue Specificity

Lambin, Jeroen; Aşçı, Sinem Demirel; Dubiel, Malgorzata; Tsaneva, Mariya Tsankova; Verbeke, Isabel; Wytynck, Pieter; Zaeytijd, Jeroen De; Smagghe, Guy; Subramanyam, Kondeti; Damme, Els J.M. Van

doi:10.3389/fpls.2020.00185

Cited by 24 publications

(24 citation statements)

References 49 publications

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“…Transgenic lines overexpressing Orysata demonstrated a higher germination rate and better growth after salt treatment in comparison with non-transformed control plants [102]. EUL proteins have been reported as drought, salt and abscisic acid responsive proteins in Arabidopsis, rice, wheat and barley [103][104][105]. Experiments with transgenic lines with reduced expression of the lectin receptor like kinases OsSIT1 and OsSIT2 revealed that these proteins play a role in the salt sensitivity as well as in plant development and productivity [106].…”

Section: Lectin Involvement In Abiotic Stress Responses and Developmementioning

confidence: 99%

130 years of Plant Lectin Research

2020

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Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. The history of lectins started with the discovery of ricin about 130 years ago but since then our understanding of lectins has dramatically changed. Over the years the research focus was shifted from 'the characterization of carbohydrate-binding proteins' to 'understanding the biological function of lectins'. Nowadays plant lectins attract a lot of attention especially because of their potential for crop improvement and biomedical research, as well as their application as tools in glycobiology. The present review aims to give an overview of plant lectins and their applications, and how the field evolved in the last decades.

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Section: Lectin Involvement In Abiotic Stress Responses and Developmementioning

confidence: 99%

130 years of Plant Lectin Research

2020

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“…Further, their localization varies according to the structures, tissues, and organelles of a given species, depending on the specific requirements and properties of the plants. For example, some nucleocytoplasmic lectins provide protective mechanisms in plants (Lannoo and Van Damme 2014) and some appear to be involved in stress signaling (Lambin et al 2020). Similarly, some legume lectins provide the receptors required for Rhizobium bacteria to bind to root hairs and to produce nodules (Laus et al 2006).…”

Section: The Role Of Lectins In Plantsmentioning

confidence: 99%

The carbon reactions of photosynthesis: role of lectins and glycoregulation

Nonomura¹,

Shevela²,

Komath³

et al. 2020

Photosynt.

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Modulation of glycoregulation in agriculture is reviewed here with emphasis on the elucidation of previously unknown pathways involving vacuolar lectins as well as a bypass of lectins that direct free sugars toward productivity. The reversible binding sequences of the endogenous lectin cycle are compared to an induced lectin bypass, as follows. (1) In the cycle, carbohydrate ligands, with similar binding specificities that compete for binding sites on lectins, are involved in the natural cycle of sugar exchanges. (2) For the bypass, tightly bound ligands that occupy lectins prevent free sugars from binding, making them available for productivity. This bypass is induced by methyl-α-D-mannopyranoside, a biochemical plant growth regulator for photosynthesis. Integration of this novel technology, with structural elements crucial for ligand binding by the lectins and with nitrogen assimilation, provides the basis for successful modulation of glycoregulation in crops for enhancement of quality and quantity.

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“…These physiological differences might be due to mutation(s) of the cis-regulatory elements in these genes. Cis-elements, including promoters, enhancers, and silencers, are very important for the regulation of gene expression [41,[55][56][57][58]. Likewise, the different expression levels of related genes in C. latifolia vs. C. capitulata might be caused by mutations in their cis-elements.…”

Section: Discussionmentioning

confidence: 99%

De novo transcriptome analysis and comparative expression profiling of genes associated with the taste-modifying protein neoculin in Curculigo latifolia and Curculigo capitulata fruits

Okubo

Terauchi

Okada

et al. 2021

Preprint

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Background Curculigo latifolia is a perennial plant endogenous to Southeast Asia whose fruits contain the taste-modifying protein neoculin, which binds to sweet receptors and makes sour fruits taste sweet. Although similar to snowdrop (Galanthus nivalis) agglutinin (GNA), which contains mannose-binding sites in its sequence and 3D structure, neoculin lacks such sites and has no lectin activity. Whether the fruits of C. latifolia and other Curculigo plants contain neoculin and/or GNA family members was unclear. Results Through de novo RNA-seq assembly of the fruits of C. latifolia and the related C. capitulata and detailed analysis of the expression patterns of neoculin and neoculin-like genes in both species, we assembled 85,697 transcripts from C. latifolia and 76,775 from C. capitulata using Trinity and annotated them using public databases. We identified 70,371 unigenes in C. latifolia and 63,704 in C. capitulata. In total, 38.6% of unigenes from C. latifolia and 42.6% from C. capitulata shared high similarity between the two species. We identified ten neoculin-related transcripts in C. latifolia and 15 in C. capitulata, encoding both the basic and acidic subunits of neoculin in both plants. We aligned these 25 transcripts and generated a phylogenetic tree. Many orthologs in the two species shared high similarity, despite the low number of common genes, suggesting that these genes likely existed before the two species diverged. The relative expression levels of these genes differed considerably between the two species: the transcripts per million (TPM) values of neoculin genes were 60 times higher in C. latifolia than in C. capitulata, whereas those of GNA family members were 15,000 times lower in C. latifolia than in C. capitulata. Conclusions The genetic diversity of neoculin-related genes strongly suggests that neoculin genes underwent duplication during evolution. The marked differences in their expression profiles between C. latifolia and C. capitulata may be due to mutations in regions involved in transcriptional regulation. Comprehensive analysis of the genes expressed in the fruits of these two Curculigo species helped elucidate the origin of neoculin at the molecular level.

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OsEUL Lectin Gene Expression in Rice: Stress Regulation, Subcellular Localization and Tissue Specificity

Cited by 24 publications

References 49 publications

130 years of Plant Lectin Research

130 years of Plant Lectin Research

The carbon reactions of photosynthesis: role of lectins and glycoregulation

De novo transcriptome analysis and comparative expression profiling of genes associated with the taste-modifying protein neoculin in Curculigo latifolia and Curculigo capitulata fruits

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