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KMID : 0380219930260050383
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Journal of Biochemistry and Molecular Biology
1993 Volume.26 No. 5 p.383 ~ p.390
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Molecular Cloning and Nucleotide Sequence of the Protease B Gene from Streptomyces griseus ATCC 10137
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Deog Hong Hwang
Jee Cheon Kim/Jae Hyeong Ko/Moon-Jin Chun and Si Myung Byun
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Abstract
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Streptomyces griseus protease B, which is a unique protease stable in the 7.5 M guanidinechloride solution, is one of the major extracellular proteases secreted by S. griseus. The gene encoding S. griseus protease B was isolated from S. griseus ATCC 10137 genomic library by using a synthetic oligonucleotide probe. Fragments containing the S. griseus pro-tease B gene were characterized by hybridization and demonstration of proteolytic activity in S. lividans. The amino acid sequence deduced from the nucleotide sequence was exactly the same as that reported by Henderson et al. (1987). This suggests that S. griseus protease B is produced as a precursor consisting of three portions: an amino-terminal pre-sequence (38 amino acid residues), a pro-sequence (76 amino acid residues), and mature protease (185 amino acid residues). However, some nucleotide sequences of the 3`-end flanking region were substantially different with the report. The G-rich 3`-end region may be responsible for the reduced expression level of protease in S. griseus ATCC 10137 compared to S. griseus K-1 and S. griseus IMRU 3449, two protease B-overproducing strains.
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