SRK (S-locus receptor kinase) is the receptor that allows stigma epidermal cells to discriminate between genetically related ('self') and genetically unrelated ('non-self') pollen in the self-incompatibility response of the Brassicaceae. SRK and its ligand, the pollen coat-localized SCR (S-locus cysteine-rich protein), are highly polymorphic, and their allele-specific interaction explains specificity in the self-incompatibility response. The present article reviews current knowledge of the role of SRK in the recognition and response phases of self-incompatibility, and highlights the new insights provided by analysis of a transgenic self-incompatible Arabidopsis thaliana model.
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Analysis of randomly mutated AlSRKb genes reveals that most loss-of-function mutations cause defects in plasma membrane localization.
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Graduate School of Agricultural Science, Tohoku University, 468-1 Aramaki Aza Aoba, Aoba-ku, Sendai, Miyagi, 980-8572, Japan.
Only very limited information is available on why some nonsynonymous variants severely alter gene function while others have no effect. To identify the characteristic features of mutations that strongly influence gene function, this study focused on SRK which encodes a highly polymorphic receptor kinase expressed in stigma papillary cells that underlies a female determinant of self-incompatibility in Brassicaceae. A set of 300 Arabidopsis thaliana transformants expressing mutated SRKb from A.
View Article and Find Full Text PDFIn Brassicaceae self-incompatibility (SI), self-pollen rejection is initiated by the haplotype specific interactions between the pollen S cysteine-rich/S-locus protein 11 (SCR/SP11) ligands and the stigma S receptor kinases (SRK). In SI, a member of the Plant U-Box (PUB) E3 ubiquitin ligases, ARM-repeat containing 1 (ARC1), is then activated by SRK in this stigma and cellular events downstream of this cause SI pollen rejection by inhibiting pollen hydration and pollen tube growth. During the transition to selfing, lost the SI components, , , and .
View Article and Find Full Text PDFSelf-incompatibility phenotypes of SRK mutants can be predicted with high accuracy.
bioRxiv
April 2024
Graduate School of Agricultural Science, Tohoku University, 468-1 Aramaki Aza Aoba, Aoba-ku, Sendai, Miyagi 980-8572, Japan.
Only very limited information is available on why some non-synonymous variants severely alter gene function while others have no effect. To identify the characteristic features of mutations that strongly influence gene function, this study focused on , which encodes a highly polymorphic receptor kinase expressed in stigma papillary cells that underlies a female determinant of self-incompatibility in Brassicaceae. A set of 299 transformants expressing mutated from was constructed and analyzed to determine the genotype and self-incompatibility phenotype of each transformant.
View Article and Find Full Text PDFA pollen selection system links self and interspecific incompatibility in the Brassicaceae.
Nat Ecol Evol
June 2024
State Key Laboratory of Nutrient Use and Management, Department of Ecology, College of Resources and Environmental Sciences, China Agricultural University, Beijing, China.
Self-incompatibility and recurrent transitions to self-compatibility have shaped the extant mating systems underlying the nonrandom mating critical for speciation in angiosperms. Linkage between self-incompatibility and speciation is illustrated by the shared pollen rejection pathway between self-incompatibility and interspecific unilateral incompatibility (UI) in the Brassicaceae. However, the pollen discrimination system that activates this shared pathway for heterospecific pollen rejection remains unknown.
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Plant Sci
June 2024
Institute of Plant Biology, National Taiwan University, Taipei, Taiwan. Electronic address:
The S-locus lectin receptor kinases (G-LecRKs) have been suggested as receptors for microbe/damage-associated molecular patterns (MAMPs/DAMPs) and to be involved in the pathogen defense responses, but the functions of most G-LecRKs in biotic stress response have not been characterized. Here, we identified a member of this family, G-LecRK-I.2, that positively regulates flg22- and Pseudomonas syringae pv.
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