Abstract
A 711-bp cDNA encoding a cysteine proteinase inhibitor (cystatin) was isolated from a cDNA library prepared from 7–10 cmSorghum bicolor seedlings. The nearly full-length cDNA clone encodes 130 amino acid residues, which include the Gln-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 inE. coli showed a strong papain-inhibitory activity.
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Communicated by J. Schell
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Li, Z., Sommer, A., Noe, C.R. et al. Molecular cloning and sequence analysis of a cDNA encoding a cysteine proteinase inhibitor fromSorghum bicolor seedlings. Molec. Gen. Genet. 251, 499–502 (1996). https://doi.org/10.1007/BF02172379
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DOI: https://doi.org/10.1007/BF02172379