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Chemical Compound Review

Thiolutin     N-(8-methyl-7-oxo-3,4-dithia- 8...

Synonyms: Acetopyrrothin, CHEMBL507026, NSC-3927, AG-H-51367, Ambotz87-11-6, ...
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Disease relevance of Acetopyrrothin


High impact information on Acetopyrrothin

  • Export ceases in either the presence of the RNA synthesis inhibitor thiolutin or in a temperature-sensitive RNA polymerase (rpb1) mutant [5].
  • We compared the results of this procedure with results obtained by two other procedures (approach to steady-state labeling and inhibition of transcription with Thiolutin) and also evaluated whether heat shock alter mRNA decay rates [6].
  • To explore the mechanism of inhibition of HUVEC adhesion to vitronectin by thiolutin, we examined the effect of this agent on intracellular cell adhesion signaling [7].
  • Protease inhibitors (MG115 and E64-D) decreased the rate of degradation of the paxillin induced by thiolutin and partially restored thiolutin-induced inhibition of HUVEC adhesion to vitronectin [7].
  • We found that the amount of paxillin in HUVECs was significantly reduced by thiolutin treatment, while those of other focal adhesion proteins including vinculin and focal adhesion kinase (FAK) were not [7].

Biological context of Acetopyrrothin

  • However, under conditions in which ribosome biogenesis was inhibited (e.g., inhibition of transcription with thiolutin, inhibition of transcription of ribosomal protein and RNA genes in a sly1-1 mutant at nonpermissive temperature, and inhibition of translation in a conditional prt1 mutant), Nmd3p remained associated with 60S subunits [8].
  • By using an episomal HSP82-lacZ fusion gene, we present evidence that lyticase and thiolutin induce heat shock gene expression at the level of transcription, whereas phenanthroline acts at a subsequent step, likely through message stabilization [9].
  • For three different genes, luciferin binding protein (lbp), luciferase (lcf), and glyceraldehyde-3-phosphate dehydrogenase (gapdh), which are circadian-regulated at the level of translation, the amounts of their mRNAs were determined by Northern blots for times up to 12.5 h following the addition of 1.5 microM thiolutin [10].

Anatomical context of Acetopyrrothin

  • In vivo experiments showed that thiolutin significantly suppressed angiogenesis induced by tumor cells (S-180), a pathological form of neovascularization, in a mouse dorsal air sac assay system [7].
  • We screened for low-molecular-weight natural products able to inhibit adhesion of human umbilical vein endothelial cells (HUVECs) to vitronectin, and pyrrothine group compounds including aureothricin, thioaurin and thiolutin were isolated from microbial culture broths [7].

Associations of Acetopyrrothin with other chemical compounds


Gene context of Acetopyrrothin

  • Third, the antibiotic thiolutin, previously demonstrated to inhibit all three yeast RNA polymerases both in vivo and in vitro, increases the RNA levels of HSP82 5- to 10-fold, those of SSA4 greater than 25-fold, and those of HSP26 greater than 50-fold under conditions in which transcription of non-heat-shock genes is blocked [9].
  • Metabolic labeling experiments showed that thiolutin enhanced degradation of paxillin in HUVECs [7].
  • Mapping of two transcription mutations (tlnI and tlnII) conferring thiolutin resistance, adjacent to dnaZ and rho in Escherichia coli [12].
  • The other mutants TLrII, TLrIIIa and TLrIIIb are resistant in rich as well as minimal media. beta-galactosidase could not be induced in TLrI and TLrII in the presence of thiolutin whereas the enzyme is constitutively synthesised in TLrIIIa and TLrIIIb irrespective of the drug [2].
  • Both pulsed and continuous applications of the RNA polymerase II inhibitor thiolutin cause a dramatic but reversible loss of bioluminescence and its overt rhythmicity in cells of the dinoflagellate Lingulodinium polyedrum (formerly Gonyaulax polyedra) [10].


  1. Thiolutin-resistant mutants of Salmonella typhimurium. Joshi, A., Verma, M., Chakravorty, M. Antimicrob. Agents Chemother. (1982) [Pubmed]
  2. Thiolutin resistant mutants of Escherichia coli are they RNA chain initiation mutants? Sivasubramanian, N., Jayaraman, R. Mol. Gen. Genet. (1976) [Pubmed]
  3. Participation of the host protein(s) in the morphogenesis of bacteriophage P22. Joshi, A., Siddiqui, J.Z., Verma, M., Chakravorty, M. Mol. Gen. Genet. (1982) [Pubmed]
  4. Regulation of biosynthesis of thiolutin and aureothricin in Streptomyces kasugaensis. Sturdíková, M., Proksa, B., Uhrín, D., Fuska, J. Folia Microbiol. (Praha) (1990) [Pubmed]
  5. A protein that shuttles between the nucleus and the cytoplasm is an important mediator of RNA export. Lee, M.S., Henry, M., Silver, P.A. Genes Dev. (1996) [Pubmed]
  6. Identification and comparison of stable and unstable mRNAs in Saccharomyces cerevisiae. Herrick, D., Parker, R., Jacobson, A. Mol. Cell. Biol. (1990) [Pubmed]
  7. Thiolutin, an inhibitor of HUVEC adhesion to vitronectin, reduces paxillin in HUVECs and suppresses tumor cell-induced angiogenesis. Minamiguchi, K., Kumagai, H., Masuda, T., Kawada, M., Ishizuka, M., Takeuchi, T. Int. J. Cancer (2001) [Pubmed]
  8. Nascent 60S ribosomal subunits enter the free pool bound by Nmd3p. Ho, J.H., Kallstrom, G., Johnson, A.W. RNA (2000) [Pubmed]
  9. The yeast heat shock response is induced by conversion of cells to spheroplasts and by potent transcriptional inhibitors. Adams, C.C., Gross, D.S. J. Bacteriol. (1991) [Pubmed]
  10. Lifetimes of mRNAs for clock-regulated proteins in a dinoflagellate. Rossini, C., Taylor, W., Fagan, T., Hastings, J.W. Chronobiol. Int. (2003) [Pubmed]
  11. RNA polymerase inhibitors with activity against rifampin-resistant mutants of Staphylococcus aureus. O'Neill, A., Oliva, B., Storey, C., Hoyle, A., Fishwick, C., Chopra, I. Antimicrob. Agents Chemother. (2000) [Pubmed]
  12. Mapping of two transcription mutations (tlnI and tlnII) conferring thiolutin resistance, adjacent to dnaZ and rho in Escherichia coli. Sivasubramanian, N., Jayaraman, R. Mol. Gen. Genet. (1980) [Pubmed]
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