Molecular cloning and sequencing of cDNA that encodes cysteine proteinase in the eggs of the silkmoth, Bombyx mori.
We have isolated and sequenced a 1,486-base-pair near full-length cDNA coding for Bombyx egg cysteine proteinase. The cDNA encodes 344 amino acid residues containing a typical signal peptide sequence (16 residues), pro-peptide (104 residues), and the sequence for mature enzyme (224 residues). Sequence alignments show that the egg cysteine proteinase is similar to lobster cysteine proteinase (61% identity), barley cysteine proteinase, Aleurain (52%), rice cysteine proteinase, Oryzain (54%), and rat cathepsin L (59%). The amino-terminal sequencing of the egg cysteine proteinase indicates that the enzyme purified as an inactive form from eggs is a pro-enzyme. Pro-egg cysteine proteinase was detected in other silkmoth tissues such as ovary, fat body, hemocyte, and hemolymph by immunoblotting.
Yamamoto
Y
Y
Department of Biology, Faculty of Liberal Arts, Yamaguchi University.
Takimoto
K
K
Izumi
S
S
Toriyama-Sakurai
M
M
Kageyama
T
T
Takahashi
S Y
SY
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D012831:Bombyx / Q000201:enzymology* / Q000235:genetics*; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000235:genetics*; D018076:DNA, Complementary / Q000032:analysis / Q000235:genetics*; D004792:Enzyme Precursors / Q000235:genetics*; D005260:Female; D008969:Molecular Sequence Data; D010063:Ovum / Q000201:enzymology / Q000502:physiology; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D004792:Enzyme Precursors; D003546:Cysteine Endopeptidases