Abstract
A 711-bp cDNA encoding a cysteine proteinase inhibitor (cystatin) was isolated from a cDNA library prepared from 7-10 cm Sorghum bicolor seedlings. The nearly full-length cDNA clone encodes 130 amino acid residues, which include the Gin-Val-Val-Ala-Gly motif, conserved among most of the known cystatins as a probable binding site for cysteine proteinases. The amino acid sequence of sorghum cystatin deduced from the cDNA clone shows significantly homology to those of other plant cystatins. The sorghum cystatin expressed in E. coli showed a strong papain-inhibitory activity.
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