Compartmentalization of S-RNase and HT-B degradation in self-incompatible Nicotiana

ARIEL GOLDRAIJ, KATSUHIKO KONDO, CHRISTOPHER LEE, NATHAN HANCOCK, MAYANDI SIVAGURU, SONIA VÁZQUEZ-SANTANA, SUNRAM KIM, THOMAS PHILLIPS, FELIPE CRUZ-GARCÍA & BRUCE MCCLURE

NATURE

Nature Publishing Group

Lugar: Londres; Año: 2006 vol. 439 p. 805 - 810

0028-0836

Pollen–pistil interactions are crucial for controlling plant mating. For example, S-RNase-based self-incompatibility prevents inbreeding in diverse angiosperm species. S-RNases are thought to function as specific cytotoxins that inhibit pollen that has an S-haplotype that matches one of those in the pistil. Thus, pollen and pistil factors interact to prevent mating between closely related individuals. Other pistil factors, such as HT-B, 4936-factor and the 120 kDa glycoprotein, are also required for pollen rejection but do not contribute to S-haplotype-specificity per se. Here we show that S-RNase is taken up and sorted to a vacuolar compartment in the pollen tubes. Antibodies to the 120 kDa glycoprotein label the compartment membrane. When the pistil does not express HT-B or 4936-factor, S-RNase remains sequestered, unable to cause rejection. Similarly, in wild-type pistils, compatible pollen tubes degrade HT-B and sequester S-RNase. We suggest that S-RNase trafficking and the stability of HT-B are central to S-specific pollen rejection.