Phosphorylation-dependent ribonuclease activity of Fra a 1 proteins

Besbes, Fatma; Franz-Oberdorf, Katrin; Schwab, Wilfried

doi:10.1016/j.jplph.2018.12.002

Cited by 14 publications

(19 citation statements)

References 82 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In-gel RNase activity assays were performed according to Yeh and Green 59 with slight modification. 20 μg recombinant S -RNase protein in standard sample buffer was electrophoresed on 12.5% SDS-PAGE without yeast RNA.…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Evolution of self-compatibility by a mutant Sm-RNase in citrus

et al. 2020

View full text Add to dashboard Cite

Self-incompatibility (SI) is an important mechanism that prevents self-fertilization and avoids inbreeding in flowering plants. The most widespread SI system utilizes S -ribonucleases ( S-RNase s) and S -locus F-boxes ( SLF s) as S -determinants. In citrus, SI is ancestral; Citrus maxima (pummelo) is self-incompatible, while Citrus reticulata (mandarin) and its hybrids are self-compatible (SC). Here we identified nine highly polymorphic pistil-specific, developmentally expressed S-RNase s from pummelo that segregate with S -haplotypes in a gametophytic manner and cluster with authentic S-RNase s. We provide evidence that these S-RNase s function as the female S -determinants in citrus. Moreover, we found that each S-RNase is linked to ~nine SLF s. Analysis of 117 citrus SLF/SLFL genes revealed clustering into 12 types and evidence that the S-RNase s and intra-haplotypic SLFs/SLFL s co-evolved. Our data are consistent with citrus having an S -locus comprising a S-RNase and several SLF s that fit the non-self-recognition model. We identified a predominant single nucleotide mutation, S m - RNase , in SC citrus, which provides a ‘natural’ loss of function. We present evidence that SI-SC transitions due to the S m -RNase, initially arose in mandarin, spreading to its hybrids and became fixed. Identification of an evolutionarily distant new genus utilizing the S -RNase-based SI system, >100 million years separated from the nearest S -RNase family, is a milestone for evolutionary comparative studies.

show abstract

Section: Methodsmentioning

confidence: 99%

“…20 μg recombinant S -RNase protein in standard sample buffer was electrophoresed on 12.5% SDS-PAGE without yeast RNA. After electrophoresis, the SDS-PAGE gel was washed, incubated, stained, and destained 59 . The gel was incubated in 0.1 M Tris-HCl containing 2.4 mg ml -1 Torulopsis utilis RNA (torula yeast RNA; Sigma) for 1 h at 37 °C.…”

Section: Methodsmentioning

confidence: 99%

Evolution of self-compatibility by a mutant Sm-RNase in citrus

et al. 2020

View full text Add to dashboard Cite

show abstract

“…Moreover, previous studies reported a high impact of GSH on protein synthesis, such as the transcription of chalcone synthase [51]. In plants, the formation of anthocyanins/ flavonoids, the expression of PR-10 genes, and the synthesis of PR-10 proteins are initiated in response to biotic and abiotic stress [12,35]. Since PR-10 proteins can bind flavonoids, it was suggested that they are also involved in the regulation of the flavonoid biosynthesis.…”

Section: Relationships Of Pr-10 Proteins Glutathione and Glutathione S-transferase Expressionmentioning

confidence: 99%

“…However, the biological function of Mal d 1 and other PR-10 proteins is still poorly understood [10]. The sequence homology of PR-10 proteins with ribonucleases from ginseng callus suggested ribonuclease activity for the entire protein family that could be affected by phosphorylation [11,12]. Multiple studies revealed the binding of several hydrophobic ligands such as cytokinins, phytosteroids, and flavonoid glycosides to members of the Bet v 1 family, suggesting binding, transport, and storage functions of the protein family (Table 1) [13][14][15][16][17].…”

Section: Introductionmentioning

confidence: 99%

Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1

Chebib

Schwab

2021

Foods

Self Cite

View full text Add to dashboard Cite

Pathogenesis-related (PR)-10 proteins, due to their particular secondary structure, can bind various ligands which could be important for their biological function. Accordingly, the PR-10 protein Mal d 1, the major apple allergen, probably also binds molecules in the hydrophobic cavity of its secondary structure, but it has not yet been investigated in this respect. In this study, various natural products found in apples such as flavonoids, glutathione (GSH), and glutathione disulfide (GSSG) were investigated as possible ligands of Mal d 1 using microscale thermophoresis. Dissociation constants of 16.39 µM, 29.51 µM, 35.79 µM, and 0.157 µM were determined for catechin, quercetin-3-O-rhamnoside, GSH, and GSSG, respectively. Molecular docking was performed to better understand the underlying binding mechanism and revealed hydrophobic interactions that stabilize the ligands within the pocket while hydrophilic interactions determine the binding of both GSH derivatives. The binding of these ligands could be important for the allergenicity of the PR-10 protein and provide further insights into its physiological role.

show abstract

“…In the diploid strawberry Fragaria vesca , 21 different paralogs of Fra a 1 have been identified in the sequence databases, , and up to 39 have been identified in the octoploid, cultivated strawberry ( Fragaria x ananassa ) . These paralogs display differential patterns of expression depending on the tissue, developmental stage, genotype, or fruit-processing method. ,,− So, focusing on the fruit, Fra a 1.01 is the most expressed isoform at the green stage, while Fra a 1.02 presents a ripening-induced pattern of expression being the most abundant isoform in the ripe receptacle. The allergenic potential of different Fra a 1 isoforms has also been studied.…”

Section: Introductionmentioning

confidence: 99%

Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits

Orozco-Navarrete

Kaczmarska

Dupeux

et al. 2019

J. Agric. Food Chem.

View full text Add to dashboard Cite

Although strawberries are highly appreciated fruits, their intake can induce allergic reactions in atopic patients. These reactions can be due to the patient's previous sensitization to the major birch pollen allergen Bet v 1, by which IgE generated in response to Bet v 1 cross-reacts with the structurally related strawberry Fra a 1 protein family. Fra a 1.02 is the most expressed paralog in ripe strawberries and is highly allergenic. To better understand the molecular mechanisms regulating this allergic response, we have determined the three-dimensional structure of Fra a 1.02 and four site-directed mutants that were designed based on their positions in potential epitopes. Fra a 1.02 and mutants conform to the START fold. We show that the cross-reactivity of all the mutant variants to IgE from patients allergic to Bet v 1 was significantly reduced without altering the conserved structural fold, so that they could potentially be used as hypoallergenic Fra a 1 variants for the generation of vaccines against strawberry allergy in atopic patients. Article pubs.acs.org/JAFC Cite This: J. Agric. Food Chem. XXXX, XXX, XXX−XXX

show abstract

Phosphorylation-dependent ribonuclease activity of Fra a 1 proteins

Cited by 14 publications

References 82 publications

Evolution of self-compatibility by a mutant Sm-RNase in citrus

Evolution of self-compatibility by a mutant Sm-RNase in citrus

Microscale Thermophoresis Reveals Oxidized Glutathione as High-Affinity Ligand of Mal d 1

Structural Bases for the Allergenicity of Fra a 1.02 in Strawberry Fruits

Contact Info

Product

Resources

About