The Arabidopsis lectin EULS3 is involved in stomatal closure

Hove, Jonas Van; Jaeger, Geert De; Winne, Nancy De; Guisez, Yves; Damme, Els J.M. Van

doi:10.1016/j.plantsci.2015.07.005

Cited by 37 publications

(27 citation statements)

References 34 publications

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“…japonica, indicating that the rice genome harbours a large set of putative lectin domains each characterized by a specific carbohydrate-recognition domain. Since experimental data points to the involvement of EULs in the plant stress response (Van Hove et al 2015; Al Atalah et al 2014a; Fouquaert et al 2009), the focus of this paper is on an in-depth molecular characterization of this lectin family in rice.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, it was shown that changes in expression levels of the lectin are accompanied with altered levels of stress resistance. Overexpression of ArathEULS3 enhanced drought resistance (Li et al 2014) and plants showed less disease symptoms after P. syringae infection compared to wild type plants or plants with lower transcript levels of the lectin gene (Van Hove et al 2015). …”

Section: Introductionmentioning

confidence: 99%

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Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa)

Schutter

Tsaneva

Kulkarni

et al. 2017

Rice

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Background: Lectins, defined as 'Proteins that can recognize and bind specific carbohydrate structures', are widespread among all kingdoms of life and play an important role in various biological processes in the cell. Most plant lectins are involved in stress signaling and/or defense. The family of Euonymus-related lectins (EULs) represents a group of stress-related lectins composed of one or two EUL domains. The latter protein domain is unique in that it is ubiquitous in land plants, suggesting an important role for these proteins. Results: Despite the availability of multiple completely sequenced rice genomes, little is known on the occurrence of lectins in rice. We identified 329 putative lectin genes in the genome of Oryza sativa subsp. japonica belonging to nine out of 12 plant lectin families. In this paper, an in-depth molecular characterization of the EUL family of rice was performed. In addition, analyses of the promoter sequences and investigation of the transcript levels for these EUL genes enabled retrieval of important information related to the function and stress responsiveness of these lectins. Finally, a comparative analysis between rice cultivars and several monocot and dicot species revealed a high degree of sequence conservation within the EUL domain as well as in the domain organization of these lectins.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa)

Schutter

Tsaneva

Kulkarni

et al. 2017

Rice

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“…In contrast to the classical lectins described above, these stress-inducible lectins are located in the nucleocytoplasmic compartments of the plant cell. Some nucleocytoplasmic lectins have been investigated in detail, and are proposed to be involved in stress signaling [22,23,24,25,26]. …”

Section: Introductionmentioning

confidence: 99%

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

Holle

Schutter

Eggermont

et al. 2017

IJMS

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Lectins are present throughout the plant kingdom and are reported to be involved in diverse biological processes. In this study, we provide a comparative analysis of the lectin families from model species in a phylogenetic framework. The analysis focuses on the different plant lectin domains identified in five representative core angiosperm genomes (Arabidopsis thaliana, Glycine max, Cucumis sativus, Oryza sativa ssp. japonica and Oryza sativa ssp. indica). The genomes were screened for genes encoding lectin domains using a combination of Basic Local Alignment Search Tool (BLAST), hidden Markov models, and InterProScan analysis. Additionally, phylogenetic relationships were investigated by constructing maximum likelihood phylogenetic trees. The results demonstrate that the majority of the lectin families are present in each of the species under study. Domain organization analysis showed that most identified proteins are multi-domain proteins, owing to the modular rearrangement of protein domains during evolution. Most of these multi-domain proteins are widespread, while others display a lineage-specific distribution. Furthermore, the phylogenetic analyses reveal that some lectin families evolved to be similar to the phylogeny of the plant species, while others share a closer evolutionary history based on the corresponding protein domain architecture. Our results yield insights into the evolutionary relationships and functional divergence of plant lectins.

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“…Further analysis revealed that the SNO-proteins identified were localized to the chloroplast, cytoplasm, cell wall, or vacuole with the majority showing localization to the chloroplast and having diverse functions in photosynthetic electron transfer and carbon utilization. In addition, several, including bifunctional inhibitor/lipid-transfer protein/seed storage 2S albumi, glutathione S-transferase, mannose-binding lectin protein, chlorophyll B-binding protein, and Beta-carbonic anhydrase, have been implicated in stomatal movement in response to stress [43][44][45][46][47]. This suggests that these proteins have important roles in stomatal function that may be regulated via S-nitrosylation.…”

Section: Guard Cell S-nitroso-proteomic Changes In Response To Flg22 mentioning

confidence: 99%

S-Nitroso-Proteome Revealed in Stomatal Guard Cell Response to Flg22

Lawrence

Gaitens

Guan

et al. 2020

IJMS

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Nitric oxide (NO) plays an important role in stomata closure induced by environmental stimuli including pathogens. During pathogen challenge, nitric oxide (NO) acts as a second messenger in guard cell signaling networks to activate downstream responses leading to stomata closure. One means by which NO's action is achieved is through the posttranslational modification of cysteine residue(s) of target proteins. Although the roles of NO have been well studied in plant tissues and seedlings, far less is known about NO signaling and, more specifically, protein S-nitrosylation (SNO) in stomatal guard cells. In this study, using iodoTMTRAQ quantitative proteomics technology, we analyzed changes in protein SNO modification in guard cells of reference plant Arabidopsis thaliana in response to flg22, an elicitor-active peptide derived from bacterial flagellin. A total of 41 SNO-modified peptides corresponding to 35 proteins were identified. The proteins cover a wide range of functions, including energy metabolism, transport, stress response, photosynthesis, and cell-cell communication. This study creates the first inventory of previously unknown NO responsive proteins in guard cell immune responses and establishes a foundation for future research toward understanding the molecular mechanisms and regulatory roles of SNO in stomata immunity against bacterial pathogens.

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The Arabidopsis lectin EULS3 is involved in stomatal closure

Cited by 37 publications

References 34 publications

Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa)

Evolutionary relationships and expression analysis of EUL domain proteins in rice (Oryza sativa)

Comparative Study of Lectin Domains in Model Species: New Insights into Evolutionary Dynamics

S-Nitroso-Proteome Revealed in Stomatal Guard Cell Response to Flg22

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