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

Compartmentalization of S-RNase and HT-B degradation in self-incompatible Nicotiana,10.1038/nature04491,Nature,Ariel Goldraij,Katsuhiko Kondo,Christop

Compartmentalization of S-RNase and HT-B degradation in self-incompatible Nicotiana   (Citations: 59)
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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 120kDa 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 120kDa 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.
Journal: Nature , vol. 439, no. 7078, pp. 805-810, 2006
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    • ...In flowering plants, cytotoxic S-RNases secreted by the pistil to selectively inhibit self-pollen have been studied (Goldraij et al., 2006; Luu et al., 2000)...
    • ...Using microscopy and immunolabelling methods, it was suggested that S-RNase was sorted to a vacuolar compartment or accumulated to the cytoplasm of all pollen-tubes in compatible pollinations but it was indistinguishable from that found in fully incompatible crosses because S-RNase cytotoxicity causes RNA degradation and unstable compartment for self-incompatiblity in plants (Goldraij et al., 2006; Luu et al., 2000)...

    Sang Gon Kimet al. The RNase activity of rice probenazole-induced protein1 (PBZ1) plays a...

    • ...Interestingly, vacuoles in pollen tubes of a Nicotiana species that displays self-incompatibility seem to act as a sequestration compartment for S-RNases during compatible pollen tube growth (Goldraij et al., 2006)...

    Alice Y. Cheunget al. Structural and functional compartmentalization in pollen tubes

    • ...A very different model has been proposed in Nicotiana where S-RNases are compartmentalized in pollen tubes and other proteins such as HT-B (a non-pollen protein) play a fundamental role in Sspecific pollen rejection, although they are not involved in determining S-pollen specificity [39]...
    • ...When a non-self pollen protein interacts with the S-RNase the HT-B protein is degraded and S-RNases remain sequestered in the vacuolar compartment [39]...

    Jorge Vieiraet al. Evolutionary patterns at the RNase based gametophytic self - incompati...

    • ...When the S-haplotype of pollen matches one of the two S-haplotypes of a diploid pistil, the pollen is recognized as self and rejected by the pistil (de Nettancourt, 2001)...

    Alejandro Raul Puertaet al. Identification and functional analysis of pistil self-incompatibility ...

    • ...Furthermore, S-RNases have been shown to enter pollen tubes in Shaplotype-independent manner, as assessed by immunolocalization studies [16,17]...
    • ...The vacuolar compartment is somehow disrupted if the pollination is incompatible, releasing S-RNases into the cytoplasm of the self pollen tube, where they exert their cytotoxic activity leading to the inhibition of pollen tube growth [16]...
    • ...According to the sequestration model, it is HT-B and not the S-RNase that is degraded (by an as yet unidentified protein) in compatible pollen tubes, whereas in incompatible crosses HT-B remains functional, causing the disruption of the vacuolar compartment and the subsequent release of the sequestered S-RNases into the cytoplasm [16,19,29]...
    • ...Previous studies have shown that S-RNases enter both compatible and incompatible pollen tubes [16,17]...
    • ...It is intriguing that while entry of S-RNases into pollen tubes has been shown microscopically for both Nicotiana [16] and S. chacoense [17], degradation of S-RNases has not been detected in compatible crosses of Nicotiana...

    Bolin Liuet al. Compatible Pollinations in Solanum chacoense Decrease Both S-RNase and...

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