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

Authors :
Goldraij, Ariel
Kondo, Katsuhiko
Lee, Christopher B.
Hancock, C. Nathan
Sivaguru, Mayandi
Vazquez-Santana, Sonia
Kim, Sunran
Phillips, Thomas E.
Cruz-Garcia, Felipe
McClure, Bruce
Source :
Nature. 2/16/2006, Vol. 439 Issue 7078, p805-810. 6p. 2 Diagrams, 3 Graphs.
Publication Year :
2006

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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00280836
Volume :
439
Issue :
7078
Database :
Academic Search Index
Journal :
Nature
Publication Type :
Academic Journal
Accession number :
19892492
Full Text :
https://doi.org/10.1038/nature04491