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The expression of serine carboxypeptidases during maturation and germination of the barley grain
- Degan, F.D., Rocher, A., Cameron-Mills, V., Wettstein, D. von.
- Proceedings of the National Academy of Sciences of the United States of America 1994 v.91 no.17 pp. 8209-8213
- Hordeum vulgare, complementary DNA, carboxypeptidases, nucleotide sequences, amino acid sequences, gene expression, messenger RNA, seed development, aleurone layer, seed germination, endosperm, immunohistochemistry, structural genes
- cDNA clones encoding three additional serine carboxypeptidases (Ser-CPs) have been isolated from a gibberellic acid-induced barley aleurone cDNA library. The three deduced Ser-CPs belong to the two-chain subfamily of Ser-CPs; they are synthesized as precursors with a putative signal peptide, propeptide, and linker peptide between the A and B chains. Their identification provides the proof for the existence of more than three Ser-CPs in cereal grains, and, based on their sequences, they may exhibit new substrate specificities. The expression of these and of the three previously isolated Ser-CPs from barley grains (CP-MI, CP-MII, and CP-MIII) has been investigated by Northern and Western analysis and RNA PCR. CP-MII is the only Ser-CP to be expressed and accumulate in the developing grain and is stored in its active form in the mature grain. All six Ser-CPs are expressed de novo in the germinating grain, in the scutellum, and/or in the aleurone. Furthermore, at least CP-MI, CP-MII, and CP-MIII are secreted into the endosperm. In addition, all Ser-CPs (except CP-MI) are also expressed in the roots and shoots of the growing seedling. This enzyme family thus appears to be ubiquitous in the barley plant, which suggests that Ser-CPs play additional roles besides their participation in the mobilization of storage proteins.