A salt- and dehydration-inducible pea gene, Cyp15a, encodes a cell-wall protein with sequence similarity to cysteine proteases.

The pea (Pisum sativum) gene Cyp15a encodes a protein with sequence similarity to cysteine proteases. Expression of Cyp15a was investigated during pea seedling development and in response to environmental stress. Cyp15a shows increased transcription and elevated mRNA levels in plant tissues that are partially dehydrated or treated with 0.6 M mannitol. Cyp15a mRNA levels also increase in seedlings treated with 0.2-0.25 M NaCl or KCl. During development, Cyp15a mRNA levels increase within 6 to 12 h in cotyledons and axes during germination and continue to increase for at least 96 h. Illumination of dark-grown seedlings increased Cyp15a mRNA abundance in elongating and non-elongating stem tissues. GA and ABA, which modulate the abundance of many seed-localized cysteine proteases, did not significantly modulate Cyp15a mRNA levels in stems. The protein encoded by Cyp15a contains a typical amino-terminal secretory targeting domain. This domain is followed by a pro-sequence containing ca. 110 amino acids that is found in other cysteine proteases. Polyclonal antibodies, directed against CYP15a, recognized both the larger pro-form and the cleaved mature form of CYP15a on western blots. Immunolocalization assays indicated that both forms of the protein are located in cell walls of stem cortical cells.