Abstract
The Ferric Uptake Regulator (FUR) is a transcription factor (TF) regulating the expression of several genes to control iron levels in prokaryotes. Members of this family of TFs share a common structural scaffold that typically comprises two regions that include a DNA binding and dimerization domains. While this structural organization is conserved, FUR proteins employ different mechanisms to bind divergent DNA binding elements and regulate gene expression in the absence or presence of regulatory metals. These findings, combined with the observations that FUR proteins display different geometries in regard to the relative orientation of the DNA binding and dimerization domains, have highlighted an expanding repertoire of molecular mechanisms controlling the activity of this family of TFs. In this chapter, we present an overview of the methods to purify, crystallize, and solve the structure of Campylobacter jejuni FUR.
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Acknowledgements
This work was supported by a CIHR grant MIC-274419. S.S. acknowledges a Ph.D. scholarship from Fonds de Recherche en Santé du Quebec.
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Sarvan, S., Couture, JF. (2017). Method for the Successful Crystallization of the Ferric Uptake Regulator from Campylobacter jejuni . In: Butcher, J., Stintzi, A. (eds) Campylobacter jejuni. Methods in Molecular Biology, vol 1512. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-6536-6_8
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DOI: https://doi.org/10.1007/978-1-4939-6536-6_8
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