Abstract
The bleomycin-binding proteins designated BLMA and BLMS, which confer resistance to bleomycin (Bm), from Bm-producing Streptomyces verticillus ATCC15003 and a methicillin-resistant Staphylococcus aureus B-26, respectively, were overexpressed in Escherichia coli. The present study showed that both BLMA and BLMS quench the antibacterial activity of Bm by the binding to the drug. To immuno-characterize the Bm-binding proteins, we constructed a monoclonal antibody against BLMA. The antibody, designated 893-12, did not cross react to BLMS and another Bm-binding protein from tallysomycin-producing Streptoalloteichus hindustanus. Although the ability of Bm to cleavage DNA was eliminated by a binding of BLMA to Bm, as shown by Sugiyama et al. [Gene 151 (1994) 11-15], the Bm-induced DNA degradation was restored by pre-incubation of BLMA with the anti-BLMA monoclonal antibody.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases*
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Amino Acid Sequence
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Antibodies, Monoclonal / immunology
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Bacterial Proteins / biosynthesis*
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Bacterial Proteins / genetics
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Bacterial Proteins / immunology
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Bacterial Proteins / metabolism
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Base Sequence
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Bleomycin / biosynthesis
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Bleomycin / metabolism*
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Bleomycin / pharmacology
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Blotting, Western
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Carrier Proteins / biosynthesis*
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Carrier Proteins / genetics
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Carrier Proteins / immunology
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Carrier Proteins / metabolism
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Escherichia coli / metabolism
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Isoelectric Point
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Methicillin Resistance
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Molecular Sequence Data
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Promoter Regions, Genetic
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Recombinant Proteins / biosynthesis
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Staphylococcus aureus / drug effects
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Staphylococcus aureus / metabolism*
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Streptomyces / metabolism*
Substances
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Antibodies, Monoclonal
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Bacterial Proteins
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Carrier Proteins
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Recombinant Proteins
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Bleomycin
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bleomycin N-acetyltransferase
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Acetyltransferases