Tenconi E, Urem M, Świątek-Połatyńska MA, Titgemeyer F, Muller Y, van Wezel G, Rigali S (2015)
Publication Status: Published
Publication Type: Journal article, Original article
Publication year: 2015
Book Volume: 464
Pages Range: 324-329
Journal Issue: 1
DOI: 10.1016/j.bbrc.2015.06.152
The global transcriptional regulator DasR connects N-acetylglucosamine (GlcNAc) utilization to the onset of morphological and chemical differentiation in the model actinomycete Streptomyces coelicolor. Previous work revealed that glucosamine-6-phosphate (GlcN-6P) acts as an allosteric effector which disables binding by DasR to its operator sites (called dre, for DasR responsive element) and allows derepression of DasR-controlled/GlcNAc-dependent genes. To unveil the mechanism by which DasR controls S. coelicolor development, we performed a series of electromobility shift assays with histidine-tagged DasR protein, which suggested that N-acetylglucosamine-6-phosphate (GlcNAc-6P) could also inhibit the formation of DasR-dre complexes and perhaps even more efficiently than GlcN-6P. The possibility that GlcNAc-6P is indeed an efficient allosteric effector of DasR was further confirmed by the high and constitutive activity of the DasR-repressed nagKA promoter in the nagA mutant, which lacks GlcNAc-6P deaminase activity and therefore accumulates GlcNAc-6P. In addition, we also observed that high concentrations of organic or inorganic phosphate enhanced binding of DasR to its recognition site, suggesting that the metabolic status of the cell could determine the selectivity of DasR in vivo, and hence its effect on the expression of its regulon.
APA:
Tenconi, E., Urem, M., Świątek-Połatyńska, M.A., Titgemeyer, F., Muller, Y., van Wezel, G., & Rigali, S. (2015). Multiple allosteric effectors control the affinity of DasR for its target sites. Biochemical and Biophysical Research Communications, 464(1), 324-329. https://doi.org/10.1016/j.bbrc.2015.06.152
MLA:
Tenconi, Elodie, et al. "Multiple allosteric effectors control the affinity of DasR for its target sites." Biochemical and Biophysical Research Communications 464.1 (2015): 324-329.
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