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Title 

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

Authors 

Soon Youl LeeSang Bae YouJi Wan LeeTae Young KimSung Uk KimSong Hae BokJoo Won Suh

Publisher 

The Korean Society for Applied Microbiology

Issue Date 

1998

Citation 

Journal of Microbiology and Biotechnology, vol. 8, no. 4, pp. 399-405

Keywords 

Peptide antibioticsPCRBacillus subtilis 713nucleotide sequence

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.

ISSN 

1017-7825

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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