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Many reports have shown the accumulation of specific proteins associated with cold acclimation in plants. However, there is a scarcity of data on the physiological and/or biochemical changes associated with deacclimation process. This study was initiated to determine protein changes specifically associated with deacclimation in Rhododendron. Current-year leaves were collected from three Rhododendron cultivars (`Chionoides', `Grumpy Yellow', and `Vulcanís Flame'; ≈4-year-old rooted cuttings) during natural non-acclimated (June), cold-acclimated (January), and deacclimated (May) state. Leaf freezing tolerance was evaluated using controlled freezing protocol (Lim et al. 1998, J. Amer. Soc. Hort. Sci. 123:246–252). Seasonal SDS-PAGE profiles exhibited a distinct accumulation of 27 kDa protein in deacclimated and nonacclimated tissues, but this protein was essentially undetectable in cold acclimated tissues of all three cultivars. Further characterization of this polypeptide, labeled as RhDAP27 (for rhododendron deacclimation protein), revealed that it has an iso-electric point of 6.5, has a compositional bias for Glu/Gln (13.9%), His (11.4%), Gly (11%), Ala (10%), Lys (8.3%), and Asp/Asn (8.1%)—hydrophilic amino acids constitutedabout 54% of the total amino acids while 40% were nonpolar, aliphatic amino acids (Gly, Ala, Val, Leu, Ile, Pro) and only 6% were aromatic amino acids (Phe and Tyr). Micro-sequencing of the four peptides produced by partial cleavage of RhDAP27 revealed a striking homology of RhDAP27 with two proteins (from Mesembryanthemum crystallinum and  Pinus taeda ) that belong to the family of ABA stress ripening/water deficit stress inducible proteins.

147 A 27-kDa Rhododendron Deacclimation Protein is Related to ABA Stress Ripening/Water Deficit Stress Inducible Family of Proteins