Characterization and expression of a novel thaumatin-like protein (CcTLP1) from papaveraceous plant Corydalis cava

Nawrot, Robert; Musidlak, Oskar; Barylski, Jakub; Nowicki, Grzegorz; Bałdysz, Sophia; Czerwoniec, Anna; Goździcka-Józefiak, Anna

doi:10.1016/j.ijbiomac.2021.08.067

Cited by 5 publications

(2 citation statements)

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“…When plants perceive a pathogenic infection, pathogenesis-related (PR) protein genes are significantly upregulated, acting as the first line of plant defense [ 1 , 2 ]. A recent study showed that 19 classes of PR proteins can be distinguished based on structural similarity and functional activity [ 1 , 4 ], of which, thaumatin-like proteins (TLPs)—the homologies of sweet-tasting thaumatin isolated from the plant Thaumatococcus daniellii —belong to the PR-5 family [ 5 , 6 ]. Growing evidence shows that TLPs are involved in resistance to a variety of fungal diseases in many species, such as Gossypium hirsutum [ 7 ], Gossypium barbadense [ 8 ], Solanum lycopersicum [ 4 , 9 ], Phyllostachys edulis [ 10 ], Ganoderma lingzhi [ 11 ], Triticum aestivum L. [ 12 , 13 ], Carya cathayensis [ 14 ], Fragaria ananassa [ 15 ], Allium sativum L. [ 16 ], Pinus radiata [ 17 ], Lentinula edodes [ 18 ], Camellia sinensis [ 19 ], Cucumis melo L. [ 20 ], Avena nuda [ 5 ], Musa acuminate [ 21 ], Manihot esculenta [ 22 ], Vitis amurensis [ 23 ], Populus szechuanica [ 24 ], Camellia sinensis [ 25 ], Piper colubrinum [ 26 ], Cynanchum komarovii [ 27 ], Castanea sativa [ 28 ], Actinidia chinensis [ 29 ], and Lyophyllum shimeji [ 30 ].…”

Section: Introductionmentioning

confidence: 99%

Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review

Feng,

Wei,

2024

Plants

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Thaumatin-like proteins (TLPs) comprise a complex and evolutionarily conserved protein family that participates in host defense and several developmental processes in plants, fungi, and animals. Importantly, TLPs are plant host defense proteins that belong to pathogenesis-related family 5 (PR-5), and growing evidence has demonstrated that they are involved in resistance to a variety of fungal diseases in many crop plants, particularly legumes. Nonetheless, the roles and underlying mechanisms of the TLP family in legumes remain unclear. The present review summarizes recent advances related to the classification, structure, and host resistance of legume TLPs to biotic and abiotic stresses; analyzes and predicts possible protein–protein interactions; and presents their roles in phytohormone response, root nodule formation, and symbiosis. The characteristics of TLPs provide them with broad prospects for plant breeding and other uses. Searching for legume TLP genetic resources and functional genes, and further research on their precise function mechanisms are necessary.

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Section: Introductionmentioning

confidence: 99%

Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review

Feng,

Wei,

2024

Plants

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“…TLP itself does not have a sweet taste, but as a member of the PR-5 gene family, TLP is associated with a broad range of growth, development, stress responses and host defenses in plants, fungi, and animals ( 16 ). The TLP1 gene expression level of medium-size plants possibly contributes to generative organ development in Corydalis cava ( 17 ). The TLP expression level in broccoli is significantly higher under salt and drought stress conditions, and transgenic plants overexpressing TLP exhibit high salt and drought tolerance ( 18 ).…”

Section: Introductionmentioning

confidence: 99%

PRMT5 regulates the polysaccharide content by controlling the splicing of thaumatin-like protein in Ganoderma lucidum

Liu,

Yang,

Yang

et al. 2023

Microbiol Spectr

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In the current study, the silencing of protein arginine methyltransferase 5 (PRMT5) decreased the polysaccharide content of Ganoderma lucidum compared to that of the wild-type (WT) strain. Furthermore, RNA-seq screening showed that the glycan degradation process-related gene thaumatin-like protein ( TLP ) was alternatively spliced in WT strains via retained introns, leading to the production of a longer TLP1 isoform and a shorter TLP2 isoform; however, only the TLP2 isoform was observed in PRMT5 i strains. Experiments examining the polysaccharide content of the TLP silencing, TLP1 overexpression (OE- TLP1 ), and TLP2 overexpression (OE- TLP2 ) transformants revealed that TLP2 plays a more important role than TLP1 in polysaccharide degradation. Through a combination of yeast two-hybrid, bimolecular fluorescence complementation and surface plasmon resonance assays, we found that TLP2 directly physically interacted with phosphoglucose isomerase (PGI), a key enzyme in polysaccharide synthesis, and thereby increased PGI activity. However, TLP1 failed to interact with PGI, and PGI activity was not affected. Further inspection showed that the polysaccharide content was decreased in the OE- TLP2 strains but not significantly changed in the OE- TLP1 strains compared with that in the WT strains. In addition, the polysaccharide content of the PRMT5-TLP -cosilenced strains was not significantly different from that of the WT strains. These results demonstrate that PRMT5 modulates TLP processing of pre-mRNA transcripts and thereby decreases the polysaccharide content. IMPORTANCE PRMT5 contributes to secondary metabolite biosynthesis in Ganoderma lucidum . However, the mechanism through which PRMT5 regulates the biosynthesis of secondary metabolites remains unclear. In the current study, PRMT5 silencing led to a significant decrease in the biosynthesis of polysaccharides from G. lucidum through the action of the alternative splicing of TLP . A shorter TLP2 isoform can directly bind to PGI and regulated polysaccharide biosynthesis. These results suggest that PRMT5 enhances PGI activity by regulating TLP binding to PGI. The results of the current study reveal a novel target gene for PRMT5-mediated alternative splicing and provide a reference for the identification of PRMT5 regulatory target genes.

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In Silico Structural and Functional Characterization of the Thaumatin‐Like Gene Family in Phaseolus lunatus Reveals the Potential for Microbial and Antiviral Activity

Matos,

Alves,

da Silva

et al. 2024

Peptide Science

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Thaumatin‐like proteins (TLPs) are part of the pathogenesis‐related (PR) proteins that are important in host plant defense. TLPs have multiple defense functions against pathogens (bacteria, viruses, and fungi) and are involved in other biological processes of several living organisms. However, the biological role of TLPs must be elucidated for other species, such as Phaseolus lunatus, popularly known as lima bean. In this study, we propose to investigate the biological activity of TLPs in P. lunatus, which can help develop a detailed functional characterization of the TLP gene in other crop cultures. As a result, a total of 31 PlTPLs genes and 16 highly conserved cysteine residues for each family member were identified in the lima bean genome. Regarding phylogenetic analysis, 128 TLPs from different plant species, including P. lunatus, were used, and the phenetic tree revealed that the TLPs could be divided into six groups. The leading group was Group 4, containing 34 TLPs; the smallest was Group 7, containing only a single TLP. The analysis of antimicrobial and antiviral activity revealed that 27 PlTLPs have antimicrobial activity and 7 PlTLPs have potential antiviral activity. For chromosomal distribution of the PlTLPs, 8 of 11 chromosomes presented at least one PlTLs on one of the chromosomes. Finally, molecular modeling was carried out between two TLPs (PlTLP5 and PlTLP14), which presented antimicrobial and antiviral activity and did not have allergenic activity. The results showed that the two candidates presented ≥90% of their residues in the favorable regions and ∼10% in the permitted regions, demonstrating that the two PlTLPs are considered promising targets for biotechnological applications, especially those related to the genetic improvement of agricultural crops and the development of antimicrobial agents.

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Characterization and expression of a novel thaumatin-like protein (CcTLP1) from papaveraceous plant Corydalis cava

Cited by 5 publications

References 76 publications

Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review

Thaumatin-like Proteins in Legumes: Functions and Potential Applications—A Review

PRMT5 regulates the polysaccharide content by controlling the splicing of thaumatin-like protein in Ganoderma lucidum

In Silico Structural and Functional Characterization of the Thaumatin‐Like Gene Family in Phaseolus lunatus Reveals the Potential for Microbial and Antiviral Activity

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