WOUND-INDUCED PROTEINASE-INHIBITORS FROM TOMATO LEAVES .2. THE CDNA-DEDUCED PRIMARY STRUCTURE OF PRE-INHIBITOR-II

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  • 1 January 1985
    • journal article
    • research article
    • Vol. 260  (11) , 6561-6564
Abstract
A c[complementary]DNA containing the complete amino acid-coding region of wound-induced tomato Inhibitor II was constructed in the plasmid pUC9. The open reading frame codes for 148 amino acids including a 25-amino acid signal sequence preceding the N-terminal lysine of the mature Inhibitor II. The Inhibitor II sequence exhibits 2 domains, one domain having a trypsin inhibitory site and the other a chymotrypsin inhibitory site, apparently evolved from a smaller gene by a process of gene duplication and elongation. The amino acid sequence of tomato leaf Inhibitor II exhibits homology with 2 small proteinase inhibitors isolated from potato tuber and an inhibitor from eggplant. The small potato tuber inhibitors are homoglous with 33 amino acids of the N-terminal domain and 19 amino acids from the C-terminal domain. Two identical nucleotide sequences of Inhibitor II cDNA in the 3'' noncoding region were present that were also found in an Inhibitor I cDNA. These include an atypical polyadenylation signal, AATAAG and a 10-base palindromic sequence, CATTATAATG, for which no function is yet known.