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KMID : 0545119960060060369
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Journal of Microbiology and Biotechnology
1996 Volume.6 No. 6 p.369 ~ p.374
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Isolation of β-Lactamase Inhibitory Protein from Streptomyces exfoliates SMF19 and Cloning of the Corresponding Gene
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PARK HYEON-UNG
LEE KYE-JOON
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Abstract
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The β-lactamase inhibitory protein (BLIP) produced by Streptomyces exfoliatus SMF19 was purified (33 kDa) and the N-terminal amino acid sequence was determined as NH2-ATSVVAWGGNND. Genomic DNA library of S. exfoliatus SMF19 was constructed in pWE15 and recombinants harbouring the corresponding gene were selected by colony hybridization to the mixture of 36-mer oligonucleotide designed from the N-terminal amino acid sequence. The corresponding gene (bliX) was isolated on a 4-kb ApaI fragment of S. exfoliatus SMF19 chromosomal DNA and then sequenced. The bliX consisting of 1,119 bp encoded a mature protein with a deduced amino acid sequence of 342 residues and also encoded a 40-amino-acid signal sequence. No signification sequence similarity to bliX was found by pairwise comparison using various protein and nucleotide sequences.
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KEYWORD
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