Thiolutin is a natural dithiol that reversibly inhibits bacterial and yeast RNA polymerases (IC50 = 3 μg/ml).1,2,3 Because of this, it can be used for the analysis of mRNA stability. Thiolutin also inhibits endothelial cell adhesion (IC50 < 1 μM) and S180 tumor-induced angiogenesis in mice by inhibiting Hsp27 interactions with cytoskeletal elements.4,5
1
Jimenez, A., Tipper, D.J., and Davies, J. Mode of action of thiolutin, an inhibitor of macromolecular synthesis in Saccharomyces cerevisiae. Antimicrob Agents Chemother 3(6) 729-738 (1973).
2
Tipper, D.J. Inhibition of yeast ribonucleic acid polymerases by thiolutin. J Bacteriol 116(1) 245-256 (1973).
3
Khachatourians, G.G., and Tipper, D.J. Inhibition of messenger ribonucleic acid synthesis in Escherichia coli by thiolutin. J Bacteriol 119(3) 795-804 (1974).
4
Dai, S., Jia, Y., Wu, S., et al. Comprehensive characterization of heat shock protein 27 phosphorylation in human endothelial cells stimulated by the microbial dithiole thiolutin. J Proteome Res 7(10) 4384-4395 (2008).
5
Jia, Y., Wu, S., Isenberg, J.S., et al. Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton. Cell Stress Chaperones 15 165-181 (2010).