Isolation and characterization of two amino acid-activating domains of peptide synthetase gene from Bacillus subtilis 713

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Title
Isolation and characterization of two amino acid-activating domains of peptide synthetase gene from Bacillus subtilis 713
Author(s)
Soon Youl Lee; Sang Bae You; Ji Wan Lee; Tae Young Kim; Sung Uk Kim; Song Hae Bok; Joo Won Suh
Bibliographic Citation
Journal of Microbiology and Biotechnology, vol. 8, no. 4, pp. 399-405
Publication Year
1998
Abstract
From the sequence alignment of various non-ribosomal 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 acid-activating 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.
Keyword
Peptide antibioticsPCRBacillus subtilis 713nucleotide sequence
ISSN
1017-7825
Publisher
Korea Soc-Assoc-Inst
Type
Article
Appears in Collections:
1. Journal Articles > Journal Articles
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