A full-length dehydrin-like cDNA clone was obtained from a Pistacia vera L. cDNA library. The clone was sequenced and it was found that the deduced protein consists of 230 amino acids with a molecular weight of 25.87 kDa. The glycine rich protein is highly hydrophilic, contains 47.4% charged amino acids and belongs to the Kn-type of dehydrins. It comprises five repetitive units, each containing the K-segment diagnostic of dehydrins, but no serine tract (S-segment) and no Y-segment. Temporally, accumulation of the dehydrin transcript coincides with accumulation of the protein, which remains high in the bud scales of the inflorescence throughout winter. The dehydrin protein accumulates in the outer leaves (scales) of the inflorescence bud and in the bark of 1-year-old stems. In the buds it is mostly concentrated in the palisade-like cells underneath the epidermis, in the bud and in the inner bark parenchyma. Immunogold labeling revealed that it is a cytoplasmic protein with no specific organellar localization. It is suggested that the dehydrin of pistachio may have a dual function, a role in drought and cold tolerances, as well as serving as a storage protein.
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Acknowledgements The technical assistance of Mrs. Mara Dek and the late Mrs. Ilana Salomon is greatly appreciated. Thanks are due to Dr. Levava Roiz for her assistance in the anatomical analyses. This work was partially supported by the Blaustein Center for Scientific Cooperation and in part under Grant No. TA-MOU-98-CA17–028 funded by the U.S.-Israel Cooperative Development Research Program, Bureau for Economic Growth, Agriculture, and Trade, U.S. Agency for International Development.
- Pistacia vera L.