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T8902 Sigma

Thiostrepton from Streptomyces azureus

≥90% (HPLC)

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Description

Application

Thiostrepton has been used as a selectable marker for recombinant Streptomyces cultures1,2,3.

Packaging

1 g in poly bottle

Preparation Note

Thiostrepton dissolves in acetic acid at 25 mg/ml to yield a clear to hazy, yellow-yellow brown solution.

Biochem/physiol Actions

Peptide antibiotic that prevents the binding of elongation factor G (EF-G) and GTP to the 50S ribosomal subunit.

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Safety & Documentation

Safety Information

Symbol 
GHS07  GHS07
Signal word 
Warning
Hazard statements 
Hazard Codes (Europe) 
Xn
Risk Statements (Europe) 
22
WGK Germany 
3
RTECS 
XN6300100

Documents

Certificate of Analysis

Certificate of Origin

Protocols & Articles

Peer-Reviewed Papers

References

Set your institution to view full text papers.

1. Characterization of the pathway-specific positive transcriptional regulator for actinorhodin biosynthesis in Streptomyces coelicolor A3(2) as a DNA-binding protein. Arias P, Fernández-Moreno MA, and Malpartida F J. Bacteriol. 181(22), 6958-68, (1999)

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2. A relA/spoT homologous gene from Streptomyces coelicolor A3(2) controls antibiotic biosynthetic genes. Martínez-Costa OH, Arias P, Romero NM, et al. J. Biol. Chem. 271(18), 10627-34, (1996)

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3. An additional regulatory gene for actinorhodin production in Streptomyces lividans involves a LysR-type transcriptional regulator. Martínez-Costa OH, Martín-Triana AJ, Martínez E, et al. J. Bacteriol. 181(14), 4353-64, (1999)

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The transcription factor FOXM1 is a cellular target of the natural product thiostrepton. Hegde NS, Sanders DA, Rodriguez R, et al. Nature Chemistry 3(9), 725-31, (2011)

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Thiostrepton is an inducer of oxidative and proteotoxic stress that impairs viability of human melanoma cells but not primary melanocytes. Qiao S, Lamore SD, Cabello CM, et al. Biochem. Pharmacol. 83(9), 1229-40, (2012)

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A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Wimberly, B.T., et al. Cell 97, 491-502, (1999)

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Broad spectrum thiopeptide recognition specificity of the Streptomyces lividans TipAL protein and its role in regulating gene expression. Chiu, M.L., et al. J. Biol. Chem. 274, 20578-20586, (1999)

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How thiostrepton was made in the laboratory. Nicolaou KC Angew. Chem. Int. Ed. Engl. 51(50), 12414-36, (2012)

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Thiostrepton tryptophan methyltransferase expands the chemistry of radical SAM enzymes. Pierre S, Guillot A, Benjdia A, et al. Nat. Chem. Biol. 8(12), 957-9, (2012)

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Principal component and clustering analysis on molecular dynamics data of the ribosomal L11·23S subdomain. Wolf A and Kirschner KN J. Mol. Model. 19(2), 539-49, (2013)

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[Bacteriocidal activity of Streptomyces cultures]. Polishchuk LV, Bambura OI, and Luk'ianchuk VV Mikrobiol. Z. 74(4), 45-51, (2012)

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[Construction of a new bifunctional vector which contains EGFP-gene]. Luk'ianchuk VV and Polishchuk LV Mikrobiol. Z. 74(2), 73-8, (2012)

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Combination with bortezomib enhances the antitumor effects of nanoparticle-encapsulated thiostrepton. Wang M and Gartel AL Cancer Biol. Ther. 13(3), 184-9, (2012)

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Mutagenesis of the thiostrepton precursor peptide at Thr7 impacts both biosynthesis and function. Li C, Zhang F, and Kelly WL Chem. Commun. (Camb.) 48(4), 558-60, (2012)

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FoxM1 knockdown sensitizes human cancer cells to proteasome inhibitor-induced apoptosis but not to autophagy. Pandit B and Gartel AL Cell Cycle 10(19), 3269-73, (2011)

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Micelle-encapsulated thiostrepton as an effective nanomedicine for inhibiting tumor growth and for suppressing FOXM1 in human xenografts. Wang M and Gartel AL Mol. Cancer Ther. 10(12), 2287-97, (2011)

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Aberrant activation of ERK/FOXM1 signaling cascade triggers the cell migration/invasion in ovarian cancer cells. Gabriel T. M. Lok et al PLoS ONE 6, e23790, (2011)

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Peroxiredoxin 3 is a redox-dependent target of thiostrepton in malignant mesothelioma cells. Newick K, Cunniff B, Preston K, et al. PLoS ONE 7(6), e39404, (2012)

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FOXM1 is an oncogenic mediator in Ewing Sarcoma. Christensen L, Joo J, Lee S, et al. PLoS ONE 8(1), e54556, (2013)

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Apicoplast-targeting antibacterials inhibit the growth of Babesia parasites. Aboulaila M, Munkhjargal T, Sivakumar T, et al. Antimicrob. Agents Chemother. 56(6), 3196-206, (2012)

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In vivo production of thiopeptide variants. Zhang F and Kelly WL Meth. Enzymol. 516, 3-24, (2012)

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Thiostrepton inhibits stable 70S ribosome binding and ribosome-dependent GTPase activation of elongation factor G and elongation factor 4. Walter JD, Hunter M, Cobb M, et al. Nucleic Acids Res. 40(1), 360-70, (2012)

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Overexpression of FoxM1 offers a promising therapeutic target in diffuse large B-cell lymphoma. Uddin S, Hussain AR, Ahmed M, et al. Haematologica 97(7), 1092-100, (2012)

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Insights into quinaldic acid moiety formation in thiostrepton biosynthesis facilitating fluorinated thiopeptide generation. Duan L, Wang S, Liao R, et al. Chem. Biol. 19(4), 443-8, (2012)

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Influence of thiostrepton binding on the ribosomal GTPase associated region characterized by molecular dynamics simulation. Wolf A, Baumann S, Arndt HD, et al. Bioorg. Med. Chem. 20(24), 7194-205, (2012)

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Thiostrepton, proteasome inhibitors and FOXM1. Gartel AL Cell Cycle 10(24), 4341-2, (2011)

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ppGpp inhibits peptide elongation cycle of chloroplast translation system in vitro. Nomura Y, Takabayashi T, Kuroda H, et al. Plant Mol. Biol. 78(1-2), 185-96, (2012)

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Proteasome inhibitors suppress expression of NPM and ARF proteins. Pandit B and Gartel AL Cell Cycle 10(22), 3827-9, (2011)

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Combination treatment with bortezomib and thiostrepton is effective against tumor formation in mouse models of DEN/PB-induced liver carcinogenesis. Wang M, Halasi M, Kabirov K, et al. Cell Cycle 11(18), 3370-2, (2012)

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Thiostrepton inhibits the turnover but not the GTPase of elongation factor G on the ribosome. Rodnina, M.V., et al. Proc. Natl. Acad. Sci. U. S. A. 96, 9586-9590, (1999)

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Development of a vector and host system and characterization of replication of plasmid pSQ10 in moderately halophilic Nocardiopsis. Zeng A, Wang T, Xia H, et al. Acta Biochim. Biophys. Sin. (Shanghai) 43(9), 738-43, (2011)

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