scholarly journals Identification of the Anti-Infective Aborycin Biosynthetic Gene Cluster from Deep-Sea-Derived Streptomyces sp. SCSIO ZS0098 Enables Production in a Heterologous Host

Marine Drugs ◽  
2019 ◽  
Vol 17 (2) ◽  
pp. 127 ◽  
Author(s):  
Mingwei Shao ◽  
Juying Ma ◽  
Qinglian Li ◽  
Jianhua Ju
Keyword(s):  
Antibacterial Activity ◽  
Gene Cluster ◽  
Deep Sea ◽  
Streptomyces Coelicolor ◽  
Biosynthetic Gene Cluster ◽  
Type I ◽  
Biosynthetic Gene ◽  
Heterologous Host ◽  
Streptomyces Sp ◽  
Enterococcus Gallinarum

Aborycin is a ribosomally synthesized member of the type I lasso peptide natural products. In the present study, aborycin was isolated and identified from the deep-sea-derived microbe Streptomyces sp. SCSIO ZS0098. The aborycin biosynthetic gene cluster (abo) was identified on the basis of genome sequence analyses and then heterologously expressed in Streptomyces coelicolor M1152 to effectively produce aborycin. Aborycin generated in this fashion exhibited moderate antibacterial activity against 13 Staphylococcus aureus strains from various sources with minimum inhibitory concentrations MICs = 8.0~128 µg/mL, against Enterococcus faecalis ATCC 29212 with an MIC = 8.0 µg/mL, and against Bacillus thuringiensis with MIC = 2.0 µg/mL. Additionally, aborycin displayed potent antibacterial activity (MIC = 0.5 µg/mL) against the poultry pathogen Enterococcus gallinarum 5F52C. The reported abo cluster clearly has the potential to provide a means of expanding the repertoire of anti-infective type I lasso peptides.

Identification of the kinanthraquinone biosynthetic gene cluster by expression of an atypical response regulator

2021 ◽  
Vol 85 (3) ◽  
pp. 714-721
Author(s):  
Risa Takao ◽  
Katsuyuki Sakai ◽  
Hiroyuki Koshino ◽  
Hiroyuki Osada ◽  
Shunji Takahashi
Keyword(s):  
Heterologous Expression ◽  
Gene Cluster ◽  
Secondary Metabolite ◽  
Response Regulator ◽  
Bac Library ◽  
Gene Clusters ◽  
Biosynthetic Gene Cluster ◽  
Gene Organization ◽  
Biosynthetic Gene ◽  
Streptomyces Sp

ABSTRACT Recent advances in genome sequencing have revealed a variety of secondary metabolite biosynthetic gene clusters in actinomycetes. Understanding the biosynthetic mechanism controlling secondary metabolite production is important for utilizing these gene clusters. In this study, we focused on the kinanthraquinone biosynthetic gene cluster, which has not been identified yet in Streptomyces sp. SN-593. Based on chemical structure, 5 type II polyketide synthase gene clusters were listed from the genome sequence of Streptomyces sp. SN-593. Among them, a candidate gene cluster was selected by comparing the gene organization with grincamycin, which is synthesized through an intermediate similar to kinanthraquinone. We initially utilized a BAC library for subcloning the kiq gene cluster, performed heterologous expression in Streptomyces lividans TK23, and identified the production of kinanthraquinone and kinanthraquinone B. We also found that heterologous expression of kiqA, which belongs to the DNA-binding response regulator OmpR family, dramatically enhanced the production of kinanthraquinones.

Cloning and characterization of the histidine biosynthetic gene cluster of Streptomyces coelicolor A3(2)

Gene ◽  
1990 ◽  
Vol 90 (1) ◽  
pp. 31-41 ◽  
Author(s):  
Danila Limauro ◽  
Alessandra Avitabile ◽  
Carmela Cappellano ◽  
Anna Maria Puglia ◽  
Carmelo B. Bruni
Keyword(s):  
Gene Cluster ◽  
Streptomyces Coelicolor ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene

Isolation and characterization of meridamycin biosynthetic gene cluster from Streptomyces sp. NRRL 30748

Gene ◽  
2006 ◽  
Vol 377 ◽  
pp. 109-118 ◽  
Author(s):  
Min He ◽  
Bradley Haltli ◽  
Mia Summers ◽  
Xidong Feng ◽  
John Hucul
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene ◽  
Streptomyces Sp ◽  
Isolation And Characterization

Activation and Characterization of Bohemamine Biosynthetic Gene Cluster from Streptomyces sp. CB02009

2020 ◽  
Vol 22 (12) ◽  
pp. 4614-4619 ◽  
Author(s):  
Ling Liu ◽  
Sainan Li ◽  
Runze Sun ◽  
Xiangjing Qin ◽  
Jianhua Ju ◽  
...  
Keyword(s):  
Gene Cluster ◽  
Biosynthetic Gene Cluster ◽  
Biosynthetic Gene ◽  
Streptomyces Sp

scholarly journals Gene Cluster Involved in the Biosynthesis of Griseobactin, a Catechol-Peptide Siderophore of Streptomyces sp. ATCC 700974

2009 ◽  
Vol 192 (2) ◽  
pp. 426-435 ◽  
Author(s):  
Silke I. Patzer ◽  
Volkmar Braun
Keyword(s):  
Gene Cluster ◽  
Linear Form ◽  
Streptomyces Griseus ◽  
Biosynthetic Gene Cluster ◽  
Peptide Structure ◽  
Biosynthetic Gene ◽  
Biosynthesis Gene Cluster ◽  
Streptomyces Sp ◽  
Peptide Synthetase ◽  
Biosynthesis Gene

ABSTRACT The main siderophores produced by streptomycetes are desferrioxamines. Here we show that Streptomyces sp. ATCC 700974 and several Streptomyces griseus strains, in addition, synthesize a hitherto unknown siderophore with a catechol-peptide structure, named griseobactin. The production is repressed by iron. We sequenced a 26-kb DNA region comprising a siderophore biosynthetic gene cluster encoding proteins similar to DhbABCEFG, which are involved in the biosynthesis of 2,3-dihydroxybenzoate (DHBA) and in the incorporation of DHBA into siderophores via a nonribosomal peptide synthetase. Adjacent to the biosynthesis genes are genes that encode proteins for the secretion, uptake, and degradation of siderophores. To correlate the gene cluster with griseobactin synthesis, the dhb genes in ATCC 700974 were disrupted. The resulting mutants no longer synthesized DHBA and griseobactin; production of both was restored by complementation with the dhb genes. Heterologous expression of the dhb genes or of the entire griseobactin biosynthesis gene cluster in the catechol-negative strain Streptomyces lividans TK23 resulted in the synthesis and secretion of DHBA or griseobactin, respectively, suggesting that these genes are sufficient for DHBA and griseobactin biosynthesis. Griseobactin was purified and characterized; its structure is consistent with a cyclic and, to a lesser extent, linear form of the trimeric ester of 2,3-dihydroxybenzoyl-arginyl-threonine complexed with aluminum under iron-limiting conditions. This is the first report identifying the gene cluster for the biosynthesis of DHBA and a catechol siderophore in Streptomyces.

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