Polymorphism of the kinase domain of the S-locus receptor kinase gene (SRK) in Brassica oleracea L.

1997 ◽  
Vol 95 (3) ◽  
pp. 335-342 ◽  
Author(s):  
T. Nishio ◽  
M. Kusaba ◽  
K. Sakamoto ◽  
D. J. Ockendon
Keyword(s):  
Brassica Oleracea ◽  
Kinase Domain ◽  
Receptor Kinase ◽  
S Locus ◽  
Kinase Gene ◽  
Brassica Oleracea L

Identification and characterization of BoPUB3: a novel interaction protein with S-locus receptor kinase in Brassica oleracea L.

2019 ◽  
Vol 51 (7) ◽  
pp. 723-733 ◽  
Author(s):  
Songmei Shi ◽  
Qiguo Gao ◽  
Tonghong Zuo ◽  
Zhenze Lei ◽  
Quanming Pu ◽  
...  
Keyword(s):  
Brassica Oleracea ◽  
Signaling Pathway ◽  
Chromosomal Region ◽  
The Self ◽  
Mature Stage ◽  
Self Incompatibility ◽  
Receptor Kinase ◽  
S Locus ◽  
Phylogenic Tree ◽  
Brassica Oleracea L

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.

scholarly journals The S locus receptor kinase gene encodes a soluble glycoprotein corresponding to the SRK extracellular domain in Brassica oleracea

1995 ◽  
Vol 8 (6) ◽  
pp. 827-834 ◽  
Author(s):  
Jean-Loïc Giranton ◽  
María José Ariza ◽  
Christian Dumas ◽  
J. Mark Cock ◽  
Thierry Gaude
Keyword(s):  
Brassica Oleracea ◽  
Extracellular Domain ◽  
Receptor Kinase ◽  
S Locus ◽  
Kinase Gene

scholarly journals Interaction of Calmodulin, a Sorting Nexin and Kinase-Associated Protein Phosphatase with the Brassica oleracea S Locus Receptor Kinase

2003 ◽  
Vol 133 (2) ◽  
pp. 919-929 ◽  
Author(s):  
Vincent Vanoosthuyse ◽  
Gabrielle Tichtinsky ◽  
Christian Dumas ◽  
Thierry Gaude ◽  
J. Mark Cock
Keyword(s):  
Brassica Oleracea ◽  
Protein Phosphatase ◽  
Receptor Kinase ◽  
S Locus ◽  
Sorting Nexin

scholarly journals Characterization of the S locus genes, SLG and SRK, of the Brassica S3 haplotype: identification of a membrane-localized protein encoded by the S locus receptor kinase gene

1995 ◽  
Vol 7 (3) ◽  
pp. 429-440 ◽  
Author(s):  
Valerie Delorme ◽  
Jean-Loic Giranton ◽  
Yves Hatzfeld ◽  
Aline Friry ◽  
Philippe Heizmann ◽  
...  
Keyword(s):  
Receptor Kinase ◽  
S Locus ◽  
Kinase Gene

scholarly journals Two members of the thioredoxin-h family interact with the kinase domain of a Brassica S locus receptor kinase.

1996 ◽  
Vol 8 (9) ◽  
pp. 1641-1650 ◽  
Author(s):  
M S Bower ◽  
D D Matias ◽  
E Fernandes-Carvalho ◽  
M Mazzurco ◽  
T Gu ◽  
...  
Keyword(s):  
Kinase Domain ◽  
Receptor Kinase ◽  
S Locus ◽  
Thioredoxin H
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