The Pollen S-determinant in Papaver: Comparisons with Known Plant Receptors and Protein Ligand Partners.

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 Ca2+-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 ;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.