ArticleJournal of bacteriology1997
Streptothricin biosynthesis is catalyzed by enzymes related to nonribosomal peptide bond formation.
Article in Journal of bacteriology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 43 citations in OpenAlex.
- History of the streptothricin antibiotics and evidence for the neglect of the streptothricin resistome.npj antimicrobials and resistance · 2024Review
- N-Formimidoylation/-iminoacetylation modification in aminoglycosides requires FAD-dependent and ligand-protein NOS bridge dual chemistry.Nature communications · 2023Article
- Production of a broad spectrum streptothricin like antibiotic from halotolerant Streptomyces fimbriatus isolate G1 associated with marine sediments.Folia microbiologica · 2021Article
- Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020Review
- Insights into the Function of theApplied and environmental microbiology · 2019Article
- In Bacillus subtilis, the SatA (Formerly YyaR) Acetyltransferase Detoxifies Streptothricin via Lysine Acetylation.Applied and environmental microbiology · 2017Article
- Development of an intergeneric conjugal transfer system for xinaomycins-producing Streptomyces noursei Xinao-4.International journal of molecular sciences · 2014Article
- A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis.Nature chemical biology · 2012Article
- Emergence of macrolide resistance gene mph(B) in Streptococcus uberis and cooperative effects with rdmC-like gene.Antimicrobial agents and chemotherapy · 2008Article
- Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics active against drug-resistant gram-positive pathogens.Antimicrobial agents and chemotherapy · 2006Article
- Inhibition of epsilon-poly-L-lysine biosynthesis in Streptomycetaceae bacteria by short-chain polyols.Applied and environmental microbiology · 2006Article
- In situ monitoring of streptothricin production by Streptomyces rochei F20 in soil and rhizosphere.Applied and environmental microbiology · 2004Article
- Deciphering tuberactinomycin biosynthesis: isolation, sequencing, and annotation of the viomycin biosynthetic gene cluster.Antimicrobial agents and chemotherapy · 2003Article
- Stenotrophomonas maltophilia D457R contains a cluster of genes from gram-positive bacteria involved in antibiotic and heavy metal resistance.Antimicrobial agents and chemotherapy · 2000Article
- A silent ABC transporter isolated from Streptomyces rochei F20 induces multidrug resistance.Journal of bacteriology · 1998Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In a search for strains producing biocides with a wide spectrum of activity, a new strain was isolated. This strain was taxonomically characterized as Streptomyces rochei F20, and the chemical structure of the bioactive product extracted from its fermentation broth was determined to be a mixture of streptothricins. From a genomic library of the producer strain prepared in the heterologous host Streptomyces lividans, a 7.2-kb DNA fragment which conferred resistance to the antibiotic was isolated. DNA sequencing of 5.2 kb from the cloned fragment revealed five open reading frames (ORFs) such that ORF1, -2, -3, and -4 were transcribed in the same direction while ORF5 was convergently arranged. The deduced product of ORF1 strongly resembled those of genes involved in peptide formation by a nonribosomal mechanism; the ORF2 product strongly resembled that of mphA and mphB isolated from Escherichia coli, which determines resistance to several macrolides by a macrolide 2'-phosphotransferase activity; the ORF3 product had similarities with several hydrolases; and the ORF5 product strongly resembled streptothricin acetyltransferases from different gram-positive and gram-negative bacteria. ORF5 was shown to be responsible for acetyl coenzyme A-dependent streptothricin acetylation. No similarities in the databases for the ORF4 product were found. Unlike other peptide synthases, that for streptothricin biosynthesis was arranged as a multienzymatic system rather than a multifunctional protein. Insertional inactivation of ORF1 and ORF2 (and to a lesser degree, of ORF3) abolishes antibiotic biosynthesis, suggesting their involvement in the streptothricin biosynthetic pathway.
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Registered trials
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