Characterization of a putative S locus encoded receptor protein and its role in self-incompatibility
Monoclonal antibodies (MAb) were raised against purified SLSG and polyclonal antisera were raised against purified trpE/SLR1 fusion proteins. MAbH8 reacts with a protein epitope on SLSG. MAbH8 and the anit-SLR1 antisera were used with immunogold labeling to show SLSG and SLR1 proteins are localized in papillar cell walls in the stigma. MAbH8 reacts with SLSG from CRM+ cells but not CRM-cells; amino acid sequence identity between the two classes was only 65%, vs. 80% within the CRM+ class. SLSG is necessary but not sufficient for self-incompatibility. Variable molecular weight (MW) SLSG proteins are derived from the same SLG gene. MW variations in both SLSG and SLR1 are due to changes in glycosylation and phosphorylation state. SLSG is not detectable in mature pollen, but is expressed during microspore development. Using a SLG probe, a gene for a putative receptor with protein kinase activity was identified.
- Research Organization:
- Cornell Univ., Ithaca, NY (USA)
- Sponsoring Organization:
- USDOE; USDOE, Washington, DC (USA)
- DOE Contract Number:
- FG02-88ER13909
- OSTI ID:
- 5736459
- Report Number(s):
- DOE/ER/13909-2; ON: DE91013858
- Country of Publication:
- United States
- Language:
- English
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550200* - Biochemistry
550300 - Cytology
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