
doi: 10.1271/bbb.65.156
pmid: 11272820
A gene (cabA) encoding a calcium-binding protein was cloned from Streptomyces ambofaciens. CabA was 180 amino acid residues long and contained four typical EF-hand motifs bearing high sequence similarity to the calcium-binding sites in calmodulin. Consistent with this, CabA showed distinct calcium-binding activity, comparable to bovine brain calmodulin. cabA was transcribed throughout growth, as found by S1 nuclease mapping. Southern hybridization experiments showed that a single copy of cabA was present in various Streptomyces species. A hypothetical relationship between CabA and aerial mycelium formation in this strain was examined, since S. ambofaciens showed calcium-dependent aerial mycelium formation. However, disruption of cabA or overexpression of cabA in S. ambofaciens caused no detectable phenotypic changes.
Calcium-Binding Proteins, Molecular Sequence Data, Single-Strand Specific DNA and RNA Endonucleases, Streptomyces, Blotting, Southern, Bacterial Proteins, Calmodulin, Animals, Calcium, Cattle, Amino Acid Sequence, EF Hand Motifs, Sequence Alignment
Calcium-Binding Proteins, Molecular Sequence Data, Single-Strand Specific DNA and RNA Endonucleases, Streptomyces, Blotting, Southern, Bacterial Proteins, Calmodulin, Animals, Calcium, Cattle, Amino Acid Sequence, EF Hand Motifs, Sequence Alignment
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