Multiple allosteric effectors control the affinity of DasR for its target sites

Journal article
(Original article)


Publication Details

Author(s): Tenconi E, Urem M, Świątek-Połatyńska MA, Titgemeyer F, Muller Y, van Wezel G, Rigali S
Journal: Biochemical and Biophysical Research Communications
Publication year: 2015
Volume: 464
Journal issue: 1
Pages range: 324-329
ISSN: 1090-2104


Abstract


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.



FAU Authors / FAU Editors

Muller, Yves Prof. Dr.
Lehrstuhl für Biotechnik (Proteinstruktur und -design)


How to cite

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://dx.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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Last updated on 2018-30-05 at 07:15