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KMID : 0545119980080040399
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Journal of Microbiology and Biotechnology
1998 Volume.8 No. 4 p.399 ~ p.405
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Isolation and Characterization of Two Amino Acid-activating Domains of Peptide Synthestase Gene from Bacillus subtilis 713
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Lee, Soon Youl
You, Sang Bae/Lee, Ji Wan/Kim, Tae Young/Kim, Sung Uk/Bok, Song Hae/Suh, Joo Won
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Abstract
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From the sequence alignment of various nonribosomal peptide synthetases, several motifs of highly conserved sequences have been identified within each domain of peptide synthetases. We designed PCR primers based on the highly conserved nucleotide sequences to amplify and isolate a ∼7.2-kb DNA fragment of the Bacillus subtilis 713 which was isolated and reported to produce an antifungal peptide compound. Nucleotide sequence analysis of 4.8 kb of the predicted amino acids revealed significant homology to various peptide synthetases over the whole sequence and also revealed two amino acidactivating domains with highly conserved Core 1 to Core 6 and spacer motif. This suggests that the isolated DNA fragment is part of a peptide synthetase gene for antifungal peptide.
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