The Papaver self-incompatibility pollen S-determinant, PrpS, functions in Arabidopsis thaliana

Curr Biol. 2012 Jan 24;22(2):154-9. doi: 10.1016/j.cub.2011.12.006. Epub 2011 Dec 29.

Abstract

Many angiosperms use specific interactions between pollen and pistil proteins as "self" recognition and/or rejection mechanisms to prevent self-fertilization. Self-incompatibility (SI) is encoded by a multiallelic S locus, comprising pollen and pistil S-determinants. In Papaver rhoeas, cognate pistil and pollen S-determinants, PrpS, a pollen-expressed transmembrane protein, and PrsS, a pistil-expressed secreted protein, interact to trigger a Ca(2+)-dependent signaling network, resulting in inhibition of pollen tube growth, cytoskeletal alterations, and programmed cell death (PCD) in incompatible pollen. We introduced the PrpS gene into Arabidopsis thaliana, a self-compatible model plant. Exposing transgenic A. thaliana pollen to recombinant Papaver PrsS protein triggered remarkably similar responses to those observed in incompatible Papaver pollen: S-specific inhibition and hallmark features of Papaver SI. Our findings demonstrate that Papaver PrpS is functional in a species with no SI system that diverged ~140 million years ago. This suggests that the Papaver SI system uses cellular targets that are, perhaps, common to all eudicots and that endogenous signaling components can be recruited to elicit a response that most likely never operated in this species. This will be of interest to biologists interested in the evolution of signaling networks in higher plants.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Actins / metabolism
  • Arabidopsis / physiology*
  • Caspase 3 / metabolism
  • Cell Death
  • Papaver / genetics*
  • Peptide Hydrolases / metabolism
  • Plant Proteins / metabolism*
  • Pollen / metabolism
  • Self-Incompatibility in Flowering Plants / genetics*

Substances

  • Actins
  • Plant Proteins
  • Peptide Hydrolases
  • Caspase 3
  • DEVDase