S-locus receptor kinase signalling

2014 ◽  
Vol 42 (2) ◽  
pp. 313-319 ◽  
Author(s):  
June B. Nasrallah ◽  
Mikhail E. Nasrallah

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.

2019 ◽  
Vol 51 (7) ◽  
pp. 723-733 ◽  
Author(s):  
Songmei Shi ◽  
Qiguo Gao ◽  
Tonghong Zuo ◽  
Zhenze Lei ◽  
Quanming Pu ◽  
...  

Abstract Armadillo repeat containing 1 (ARC1) is phosphorylated by S-locus receptor kinase (SRK) and functions as a positive regulator in self-incompatibility response of Brassica. However, ARC1 only causes partial breakdown of the self-incompatibility response, and other SRK downstream factors may also participate in the self-incompatibility signaling pathway. In the present study, to search for SRK downstream targets, a plant U-box protein 3 (BoPUB3) was identified from the stigma of Brassica oleracea L. BoPUB3 was highly expressed in the stigma, and its expression was increased with the stigma development and reached to the highest level in the mature-stage stigma. BoPUB3, a 76.8-kDa protein with 697 amino acids, is a member of the PUB-ARM family and contains three domain characteristics of BoARC1, including a U-box N-terminal domain, a U-box motif, and a C-terminal arm repeat domain. The phylogenic tree showed that BoPUB3 was close to BoARC1. The synteny analysis revealed that B. oleracea chromosomal region containing BoPUB3 had high synteny with the Arabidopsis thaliana chromosomal region containing AtPUB3 (At3G54790). In addition, the subcellular localization analysis showed that BoPUB3 primarily localized in the plasma membrane and also in the cytoplasm. The combination of the yeast two-hybrid and in vitro binding assay showed that both BoPUB3 and BoARC1 could interact with SRK kinase domain, and SRK showed much higher level of β-galactosidase activity in its interaction with BoPUB3 than with BoARC1. These results implied that BoPUB3 is a novel interactor with SRK, which lays a basis for further research on whether PUB3 participates in the self-incompatibility signaling pathway.


2014 ◽  
Vol 26 (12) ◽  
pp. 4749-4762 ◽  
Author(s):  
Masaya Yamamoto ◽  
Titima Tantikanjana ◽  
Takeshi Nishio ◽  
Mikhail E. Nasrallah ◽  
June B. Nasrallah

1998 ◽  
Vol 10 (2) ◽  
pp. 209-218 ◽  
Author(s):  
Richard J. Stahl ◽  
MaryAnne Arnoldo ◽  
Tracy L. Glavin ◽  
Daphne R. Goring ◽  
Steven J. Rothstein

Genetics ◽  
2001 ◽  
Vol 159 (2) ◽  
pp. 811-822
Author(s):  
Christine Miege ◽  
Véronique Ruffio-Châble ◽  
Mikkel H Schierup ◽  
Didier Cabrillac ◽  
Christian Dumas ◽  
...  

Abstract The S locus receptor kinase and the S locus glycoproteins are encoded by genes located at the S locus, which controls the self-incompatibility response in Brassica. In class II self-incompatibility haplotypes, S locus glycoproteins can be encoded by two different genes, SLGA and SLGB. In this study, we analyzed the sequences of these genes in several independently isolated plants, all of which carry the same S haplotype (S2). Two groups of S2 haplotypes could be distinguished depending on whether SRK was associated with SLGA or SLGB. Surprisingly, SRK alleles from the two groups could be distinguished at the sequence level, suggesting that recombination rarely occurs between haplotypes of the two groups. An analysis of the distribution of polymorphisms along the S domain of SRK showed that hypervariable domains I and II tend to be conserved within haplotypes but to be highly variable between haplotypes. This is consistent with these domains playing a role in the determination of haplotype specificity.


1998 ◽  
Vol 10 (2) ◽  
pp. 209
Author(s):  
Richard J. Stahl ◽  
Mary Anne Arnoldo ◽  
Tracy L. Glavin ◽  
Daphne R. Goring ◽  
Steven J. Rothstein

2009 ◽  
Vol 21 (9) ◽  
pp. 2642-2654 ◽  
Author(s):  
Titima Tantikanjana ◽  
Noreen Rizvi ◽  
Mikhail E. Nasrallah ◽  
June B. Nasrallah

2020 ◽  
Author(s):  
Patrick Kenney ◽  
Subramanian Sankaranarayanan ◽  
Michael Balogh ◽  
Emily Indriolo

AbstractMembers of the Brassicaceae family have the ability to regulate pollination events occurring on the stigma surface. In Brassica species, self-pollination leads to an allele specific interaction between the pollen small cysteine-rich peptide ligand (SCR/SP11) and the stigmatic S-receptor kinase (SRK) that activates the E3 ubiquitin ligase ARC1 (Armadillo repeat-containing 1), resulting in proteasomal degradation of various compatibility factors including Glyoxalase I (GLO1) which is necessary for successful pollination. Suppression of GLO1 was sufficient to reduce compatibility, and overexpression of GLO1 in self-incompatible Brassica napus stigmas resulted in partial breakdown of the self-incompatibility response. Here, we verified if BnGLO1 could function as a compatibility factor in the artificial self-incompatibility system of Arabidopsis thaliana expressing AlSCRb, AlSRKb and AlARC1 proteins from A. lyrata. Overexpression of BnGLO1 is sufficient to breakdown self-incompatibility response in A. thaliana stigmas, suggesting that GLO1 functions as an inter-species compatibility factor. Therefore, GLO1 has an indisputable role as a compatibility factor in the stigma in regulating pollen attachment and pollen tube growth. Lastly, this study demonstrates the usefulness of an artificial self-incompatibility system in A. thaliana for interspecific self-incompatibility studies.


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