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Compartmentalization of S-RNase and HT-B degradation in self-incompatible Nicotiana.
- 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]
- Subjects :
- *RIBONUCLEASES
*ANGIOSPERMS
*TOXINS
*POLLEN
*GLYCOPROTEINS
*POLLEN tube
Subjects
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