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

Ariel Goldraij, Katsuhiko Kondo, Christopher B. Lee, C. Nathan Hancock, Mayandi Sivaguru, Sonia Vazquez-Santana, Sunran Kim, Thomas E. Phillips, Felipe Cruz-Garcia and Bruce McClure ()
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Ariel Goldraij: Universidad Nacional de Cordoba, Ciudad Universitaria
Katsuhiko Kondo: 105 Life Sciences Center
Christopher B. Lee: 105 Life Sciences Center
C. Nathan Hancock: 4505 Miller Plant Sciences Building
Mayandi Sivaguru: Division of Biological Sciences
Sonia Vazquez-Santana: Universidad Nacional Autonoma de Mexico
Sunran Kim: 105 Life Sciences Center
Thomas E. Phillips: Division of Biological Sciences
Felipe Cruz-Garcia: Universidad Nacional Autonoma de Mexico
Bruce McClure: 105 Life Sciences Center

Nature, 2006, vol. 439, issue 7078, 805-810

Abstract: Abstract 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.

Date: 2006
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DOI: 10.1038/nature04491

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