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During the past several years we have been involved in identifying seasonally regulated proteins and genes from peach bark. In the present study, we describe the cloning of a protease inhibitor from a cDNA library made from winter bark tissues. A partial clone obtained from the library was extended to full length by 5' RACE. The full-length cDNA clone (final3b) is 613 bp in length, not including the poly A+ tail. The open reading frame of 237 bp codes for a 79 amino acid protease inhibitor related to the defensin family of proteins. This family of small, cysteine-rich, extracellular proteins play a role in the plantís defense response through their antifungal properties. Sequence comparison of the encoded protein using BLAST analysis revealed significant homology to protease inhibitors from  Glycine max, Arabidopsis thaliana , and a defensin protein from bell pepper ( Capsicum annuum ). Similar to these other cysteine-rich proteins, the peach defensin contains a consensus cys arrangement and is predicted to have an amino terminal signal peptide, presumably targeting it for extracellular transport. RNA-blot analysis indicated that the gene is seasonally expressed in bark tissues of 1-year-old shoots. Transcript abundance of final3b increased in the fall, reached a peak in midwinter and then decreased. The gene was also expressed during early stages of fruit development. RNA-blot analysis of the gene in other tissues, and in response to environmental stress and wounding, is in progress.

058 Cloning of a Defensin-related Gene and Its Expression during Dormancy and Fruit Development in Peach [Prunus persica (L.) Batsch]