A relA/spoT Homologous Gene from Streptomyces coelicolor A3(2) Controls Antibiotic Biosynthetic Genes (*)

@article{MartnezCosta1996ARH,
  title={A relA/spoT Homologous Gene from Streptomyces coelicolor A3(2) Controls Antibiotic Biosynthetic Genes (*)},
  author={O. Mart{\'i}nez-Costa and P. Arias and N. M. Romero and V. Parro and R. Mellado and F. Malpartida},
  journal={The Journal of Biological Chemistry},
  year={1996},
  volume={271},
  pages={10627 - 10634}
}
A 0.972-kilobase pair DNA fragment from Streptomyces lividans that induces the production of the blue-pigmented antibiotic actinorhodine in S. lividans when cloned on a multicopy plasmid has led to the isolation of a 4-kilobase pair DNA fragment from Streptomyces coelicolor containing homologous sequence. Computer-assisted analysis of the DNA sequence revealed three putative open reading frames (ORFs), ORF1, ORF2, and ORF3. ORF2 extends beyond the sequenced DNA fragment, and its deduced product… Expand
Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis.
TLDR
In vitro biochemical data indicate that purified RelMtb is a ribosome- and tRNA-independent ATP:GTP/GDP/ITP 3'-pyrophosphoryltransferase, and in vivo reactions were assessed in vivo in E. coli deleted in both the relA and spoT genes, which generates a (p)ppGpp0 phenotype. Expand
Molecular and Functional Analyses of the Gene (eshA) Encoding the 52-Kilodalton Protein ofStreptomyces coelicolor A3(2) Required for Antibiotic Production
  • S. Kawamoto, Masakatsu Watanabe, +4 authors K. Ochi
  • Medicine, Biology
  • Journal of bacteriology
  • 2001
TLDR
Analysis of proteins recovered in the S100 precipitate fraction of Streptomyces griseus after ultracentrifugation led to the identification of a 52-kDa protein which is produced during the late growth phase, characterized by a central region that shows homology to the eukaryotic-type cyclic nucleotide-binding domains. Expand
Molecular analysis of the ribosomal L11 protein gene (rplK = relC ) of Streptomyces griseus and identification of a deletion allele
TLDR
Propagation of the mutant rplK gene in the wild-type strain resulted in marked defects in growth, streptomycin production, and aerial mycelium formation, indicating that the mutant L11 protein exerts certain negative effects in the cells. Expand
A polyketide biosynthetic gene cluster from Streptomyces antibioticus includes a LysR-type transcriptional regulator.
TLDR
DNA binding assays and transcriptional analysis suggest that the pathway-specific regulator for actinorhodin biosynthesis (actII-ORF4) is also involved in the expression of the cloned PKS in the host strain. Expand
The promoter of a cold-shock-like gene has pleiotropic effects on Streptomyces antibiotic biosynthesis.
TLDR
Interestingly, the csp1-groEL2 region pleiotropically regulates the production of antibiotics from Streptomyces coelicolor and StrePTomyces nodosus. Expand
The role of the Corynebacterium glutamicum rel gene in (p)ppGpp metabolism.
TLDR
To investigate the metabolism of (p)ppGpp in amino-acid-producing coryneform bacteria, a PCR-based strategy using degenerate consensus oligonucleotides was applied to isolate the rel gene of Corynebacterium glutamicum ATCC 13032, which revealed extensive similarities to the related proteins RelA and SpoT of Escherichia coli. Expand
Comparative genomics and evolution of genes encoding bacterial (p)ppGpp synthetases/hydrolases (the Rel, RelA and SpoT proteins).
  • G. Mittenhuber
  • Biology, Medicine
  • Journal of molecular microbiology and biotechnology
  • 2001
TLDR
The distribution pattern of the paralogous RelA and SpoT proteins supports a new model of linear bacterial evolution, which postulates that the gamma subdivision of proteobacteria represents the most recently evolved bacterial lineage. Expand
Characterization of the Pathway-Specific Positive Transcriptional Regulator for Actinorhodin Biosynthesis inStreptomyces coelicolor A3(2) as a DNA-Binding Protein
TLDR
Although both gene products (wild-type and mutant ActII-ORF4) showed DNA-binding activity, only the wild-type gene was capable of activating transcription of the act genes; thus, two basic functions can be differentiated within the regulatory protein. Expand
Molecular and functional analysis of the ribosomal L11 and S12 protein genes (rplK and rpsL) of Streptomyces coelicolor A3(2)
TLDR
Allele replacement by gene homogenotization demonstrated that the RelC mutation is responsible for the resistance to thiostrepton and the inactivation of ppGpp, actinorhodin and undecylprodigiosin production, and could be rescued by the introduction of mutations that confer resistance to streptomycin. Expand
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Nucleotide sequence and deduced functions of a set of cotranscribed genes of Streptomyces coelicolor A3(2) including the polyketide synthase for the antibiotic actinorhodin.
TLDR
The data show that the actinorhodin PKS consists of discrete monofunctional components, like that of the Escherichia coli (Type II) FAS, rather than the multifunctional polypeptides for the macrolide PKSs and vertebrate FASs (Type I). Expand
abaA, a new pleiotropic regulatory locus for antibiotic production in Streptomyces coelicolor
TLDR
Subcloning experiments revealed that ORFB together with 137 bp downstream of it is responsible for antibiotic overproduction in S. lividans, and abaA constitutes a new locus which, like the afs and abs genes previously described, pleiotropically regulates antibiotic production. Expand
Primary structure of AfsR, a global regulatory protein for secondary metabolite formation in Streptomyces coelicolor A3(2).
TLDR
Data suggest that the AfsR protein comprises two domains, viz., an ATP-binding and a DNA-binding domain, each of which could function as a positive regulator for pigment production. Expand
DNA sequence and functions of the actVI region of the actinorhodin biosynthetic gene cluster of Streptomyces coelicolor A3(2).
TLDR
Findings strongly suggest that the actVI region is involved in catalyzing reduction processes that determine the two stereochemical configurations at C-3/C-15 during actinorhodin biosynthesis. Expand
A putative two-component regulatory system involved in secondary metabolism in Streptomyces spp.
TLDR
An amino acid replacement from Asp to Glu at residue 52 of AfsQ1, generated by site-directed mutagenesis, resulted in loss of the protein's ability to stimulate antibiotic production in S. lividans. Expand
Pleiotropic morphological and antibiotic deficiencies result from mutations in a gene encoding a tRNA-like product in Streptomyces coelicolor A3(2).
TLDR
It is postulated that bldA specifies a tRNA that would recognize the codon UUA (for leucine), which is very rare in Streptomyces genes and generally contain greater than 70 mole% (G + C], suggesting a possible role for bld a in translational control of development. Expand
afsR2: a previously undetected gene encoding a 63‐amino‐acid protein that stimulates antibiotic production in Streptomyces lividans
TLDR
The existence of a previously unknown gene, afsR2, which is separate from and adjacent to the AfsR‐encoding sequence and which, when present at high copy number, stimulates transcription of biosynthetic and regulatory genes in the actinorhodin gene cluster (act), is reported. Expand
Cloning and expression in a heterologous host of the complete set of genes for biosynthesis of the Streptomyces coelicolor antibiotic undecylprodigiosin.
TLDR
Isolation of antibiotic biosynthetic genes by the effects of an activator in a self-cloning experiment, and in vivo reconstitution of a large cluster of genes by homologous recombination, may turn out to be usefully generalizable procedures. Expand
The nucleotide sequence and characterization of the relA gene of Escherichia coli.
TLDR
The sequence of the relA gene region and assignment of its 743-codon open reading frame is presented by the following criteria: genetic complementation of ppGpp synthesis in a relaxed (relA1) mutant during the stringent response; changes in 3-aminotriazole resistance during growth to mimic a relA+ phenotype. Expand
Nucleotide sequence and transcriptional analysis of the redD locus of Streptomyces coelicolor A3(2)
TLDR
The putative redD polypeptide lacked any strong sequence similarities to other known proteins and was not involved in the regulation of undecylprodigiosin (Red) biosynthesis in Streptomyces coelicolor. Expand
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