Diversity of genes encoding nonribosomal peptide synthetases in the Streptomyces sioyaensis genome

Diversity of genes encoding nonribosomal peptide synthetases in the Streptomyces sioyaensis genome Streptomyces sioyaensis Lv81 produces siomycin, a thiopeptide antibiotic synthesized on ribosomes. Nothing is known about the ability of this strain to produce nonribosomal peptides, a well represented group of natural actinomycete compounds. Using degenerate primers, we cloned a number of DNA fragments encoding putative adenylation domains (A domains) of nonribisomal peptide synthetases involved in biosynthesis of unknown compounds. Sequencing of amplicons revealed nine different A domains, which were analyzed in more detail. Nonribosomal codes of these domains were determined, but in most cases their substrate specificity failed to be unambiguously predicted. This means that many of these domains can recognize novel amino acids and be used to improve and expand the bioinformatic toolbox applied to predict substrate specificity of A domains. Multiple sequence alingments showed that the cloned A domains are probably involved in different biosynthetic pathways. Five A domains were used in gene inactivation experiments. Inactivation of one of them (in strain 736) resulted in a decrease of the total antibiotic activity as compared to the initial strain. Other A-domain mutants were similar to the initial strain in morphology and siomycin production. The causes of reduced antibiotic activity of strain 736 are discussed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Russian Journal of Genetics Springer Journals

Diversity of genes encoding nonribosomal peptide synthetases in the Streptomyces sioyaensis genome

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Publisher
Springer Journals
Copyright
Copyright © 2010 by Pleiades Publishing, Ltd.
Subject
Biomedicine; Microbial Genetics and Genomics; Animal Genetics and Genomics; Human Genetics
ISSN
1022-7954
eISSN
1608-3369
D.O.I.
10.1134/S1022795410070033
Publisher site
See Article on Publisher Site

Abstract

Streptomyces sioyaensis Lv81 produces siomycin, a thiopeptide antibiotic synthesized on ribosomes. Nothing is known about the ability of this strain to produce nonribosomal peptides, a well represented group of natural actinomycete compounds. Using degenerate primers, we cloned a number of DNA fragments encoding putative adenylation domains (A domains) of nonribisomal peptide synthetases involved in biosynthesis of unknown compounds. Sequencing of amplicons revealed nine different A domains, which were analyzed in more detail. Nonribosomal codes of these domains were determined, but in most cases their substrate specificity failed to be unambiguously predicted. This means that many of these domains can recognize novel amino acids and be used to improve and expand the bioinformatic toolbox applied to predict substrate specificity of A domains. Multiple sequence alingments showed that the cloned A domains are probably involved in different biosynthetic pathways. Five A domains were used in gene inactivation experiments. Inactivation of one of them (in strain 736) resulted in a decrease of the total antibiotic activity as compared to the initial strain. Other A-domain mutants were similar to the initial strain in morphology and siomycin production. The causes of reduced antibiotic activity of strain 736 are discussed.

Journal

Russian Journal of GeneticsSpringer Journals

Published: Jul 22, 2010

References

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