Title: Petunia hybrida s-proteins - ribonuclease activity and the role of their glycan side chains in self-incompatibility
Authors: Broothaerts, W ×
Vanvinckenroye, P
Decock, B
Van Damme, Jozef
Vendrig, J C #
Issue Date: Oct-1991
Publisher: Springer verlag
Series Title: Sexual plant reproduction vol:4 issue:4 pages:258-66
Abstract: Self-incompatibility in flowering plants is controlled by the S-gene, encoding stylar S (allele-specific) glycoproteins. In addition to three previously characterized Petunia hybrida S-proteins, we identified by N-terminal sequence analysis another stylar S-protein, co-segregating with the S(b)-allele. Purified S-proteins reveal biological activity, as is demonstrated for two of them by the allele-specific inhibition of pollen tube growth in vitro. Moreover, the four isolated S-proteins are ribonucleases (S-RNases). Specific activities vary from 30 (S1) to 1000 (S2) units per min per mg protein. We attempted to investigate the functionality of the carbohydrate portion of the S-RNases. Deglycosylation studies with the enzyme peptide-N-glycosidase F (PNGase F) reveals differences in the number of N-linked glycan chains present on the four S-RNases. Variability in the extent of glycosylation accounts for most of the molecular weight differences observed among these proteins. By amino acid sequencing, the positions of two of the three N-glycosylation sites on the S2-RNase could be located near the N-terminus. Enzymic removal of the glycan side chains has no effect on the RNase activity of native S-RNases. This suggests another role of the glycan moiety in the self-incompatibility mechanism.
ISSN: 0934-0882
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Academic Center for General Practice
Laboratory of Molecular Immunology (Rega Institute)
× corresponding author
# (joint) last author

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