Affiliation:
1. Department of Plant Biology, Cornell University, Ithaca, New York 14853
Abstract
Abstract
The S-locus-encoded S receptor kinase (SRK) is an intrinsic plasma membrane protein that is viewed as the primary stigma determinant of specificity in the self-incompatibility response ofBrassica spp. We analyzed two self-compatible mutant strains that express low levels of the S-locus glycoprotein (SLG), a cell wall-localized protein also encoded at theS locus that is coordinately expressed with SRK. We found that mutant stigmas synthesized wild-type levels ofSRK transcripts but failed to produce SRK protein at any of the developmental stages analyzed. Furthermore, SRK was shown to form aberrant high-molecular mass aggregates when expressed alone in transgenic tobacco (Nicotiana tabacum) plants. This aggregation was prevented in tobacco plants that co-expressed SRK and SLG, but not in tobacco plants that co-expressed SRK and SLR1, an SLG-related secreted protein not encoded at the S locus. In analyses of protein extracts under reducing and non-reducing conditions, evidence of intermolecular association was obtained only for SLG, a fraction of which formed disulfide-linked oligomers and was membrane associated. The data indicate that, at least in plants carrying the S haplotypes we analyzed, SRK is an inherently unstable protein and that SLG facilitates its accumulation to physiologically relevant levels in Brassicastigmas.
Publisher
Oxford University Press (OUP)
Subject
Plant Science,Genetics,Physiology
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