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A novel inhibitor protein for Bombyx cysteine proteinase is homologous to propeptide regions of cysteine proteinases
Author(s) -
Yamamoto Yoshimi,
Watabe Shoji,
Kageyama Takashi,
Takahashi Susumu Y
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00382-8
Subject(s) - cysteine , complementary dna , biochemistry , open reading frame , peptide sequence , protein precursor , signal peptide , microbiology and biotechnology , bombyx mori , biology , amino acid , protein superfamily , chemistry , gene , enzyme
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.