title: Immunodetection of protein glycoforms encoded by two independent genes of the self-incompatibility multigene family of brassica.
abstract: Glycoprotein products of two highly homologous Brassica S gene family members were studied: SLSG (S locus-specific glycoprotein), product of an SLG gene at the S locus, and SLR1 (S locus-related) protein, product of the SLR1 gene, a gene unlinked to the S locus. A polyclonal antibody directed against a trpE-SLR1 fusion protein facilitated study of the SLR1 protein. SLR1 protein was detected in a number of crucifer species. No variation in the level of this protein was found between self-compatible and self-incompatible plants. Both SLSG and SLR1 protein occurred as glycoforms on sodium dodecyl sulfate-polyacrylamide gel electrophoresis gels. Each glycoform had several charge forms, indicated by elution patterns from a high performance liquid chromatography cation exchange column and behavior on two-dimensional gels. Deglycosylation of both SLSG and SLR1 protein caused loss of the glycoforms, which apparently arose from differences in glycosylation. Consistent with their apparent similar post-translational processing, immunolocalization showed that SLR1 protein, like SLSG, accumulated in the stigma papillae cell walls. Thus, both SLSG and SLR1 protein are present at the site of pollen-stigma interaction.
authors: Section of Plant Biology, Division of Biological Sciences, Cornell University, Ithaca, New York 14853.
authors: A L
authors: AL
authors: Umbach
authors: B A
authors: BA
authors: Lalonde
authors: M K
authors: MK
authors: Kandasamy
authors: J B
authors: JB
authors: Nasrallah
authors: M E
authors: ME
authors: Nasrallah