A novel inhibitor protein for Bombyx cysteine proteinase is homologous to propeptide regions of cysteine proteinases.
A cDNA clone for an inhibitor of Bombyx cysteine proteinase was isolated and sequenced. Active inhibitor proteins were expressed in Escherichia coli using the cDNA. The open reading frame of the cDNA encodes a 105 residues protein with 19 residues of a signal sequence. The inhibitor has amino acid sequences homologous to several cysteine proteinases, but only to their propeptide sequences. The results suggest that some cysteine proteinase proregions may have evolved as autonomous modules and become inhibitor proteins for cysteine proteinases.
Yamamoto
Y
Y
Department of Biochemistry and Radiation Biology, College of Agriculture, Yamaguchi University, Japan. yamataka@po.yb.cc.yamaguchi-u.ac.jp
Watabe
S
S
Kageyama
T
T
Takahashi
S Y
SY
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D012831:Bombyx / Q000201:enzymology*; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000737:chemistry*; D015853:Cysteine Proteinase Inhibitors / Q000235:genetics*; D016208:Databases, Factual; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000235:genetics; D008957:Models, Genetic; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid
D015853:Cysteine Proteinase Inhibitors; D003546:Cysteine Endopeptidases