The pollen S-determinant in Papaver: comparisons with known plant receptors and protein ligand partners

Abstract

Cell-cell communication is vital to multicellular organisms and much of it is controlled by the interactions of secreted protein ligands (or other molecules) with cell surface receptors. In plants, receptor-ligand interactions are known to control phenomena as diverse as floral abscission, shoot apical meristem maintenance, wound response, and self-incompatibility (SI). SI, in which 'self' (incompatible) pollen is rejected, is a classic cell-cell recognition system. Genetic control of SI is maintained by an S-locus, in which male (pollen) and female (pistil) S-determinants are encoded. In Papaver rhoeas, PrsS proteins encoded by the pistil S-determinant interact with incompatible pollen to effect inhibition of pollen growth via a Ca(2+)-dependent signalling network, resulting in programmed cell death of 'self' pollen. Recent studies are described here that identified and characterized the pollen S-determinant of SI in P. rhoeas. Cloning of three alleles of a highly polymorphic pollen-expressed gene, PrpS, which is linked to pistil-expressed PrsS revealed that PrpS encodes a novel approximately 20 kDa transmembrane protein. Use of antisense oligodeoxynucleotides provided data showing that PrpS functions in SI and is the pollen S-determinant. Identification of PrpS represents a milestone in the SI field. The nature of PrpS suggests that it belongs to a novel class of 'receptor' proteins. This opens up new questions about plant 'receptor'-ligand pairs, and PrpS-PrsS have been examined in the light of what is known about other receptors and their protein-ligand pairs in plants.