Molecular cloning and sequence analysis of a cDNA encoding a cysteine proteinase inhibitor from Sorghum bicolor seedlings.
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.
Li
Z
Z
Institut für Pharmazeutische Chemie der Johann Wolfgang Goethe-Universität, Frankfurt, Germany.
Sommer
A
A
Dingermann
T
T
Noe
C R
CR
D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D015853:Cysteine Proteinase Inhibitors / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D018076:DNA, Complementary / Q000737:chemistry; D002523:Edible Grain / Q000737:chemistry / Q000235:genetics*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008969:Molecular Sequence Data; D010206:Papain / Q000037:antagonists & inhibitors; D010940:Plant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D012639:Seeds / Q000737:chemistry; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D015853:Cysteine Proteinase Inhibitors; D018076:DNA, Complementary; D010940:Plant Proteins; D011994:Recombinant Proteins; D010206:Papain