Denby, K. J. and Iwig, J. and Bisson, C. and Westwood, J. and Rolfe, M. D. and Sedelnikova, S. E. and Higgins, K. and Maroney, M. J. and Baker, P. J. and Chivers, P. T. and Green, J. (2016) 'The mechanism of a formaldehyde-sensing transcriptional regulator.', Scientific reports., 6 . p. 38879.
Most organisms are exposed to the genotoxic chemical formaldehyde, either from endogenous or environmental sources. Therefore, biology has evolved systems to perceive and detoxify formaldehyde. The frmRA(B) operon that is present in many bacteria represents one such system. The FrmR protein is a transcriptional repressor that is specifically inactivated in the presence of formaldehyde, permitting expression of the formaldehyde detoxification machinery (FrmA and FrmB, when the latter is present). The X-ray structure of the formaldehyde-treated Escherichia coli FrmR (EcFrmR) protein reveals the formation of methylene bridges that link adjacent Pro2 and Cys35 residues in the EcFrmR tetramer. Methylene bridge formation has profound effects on the pattern of surface charge of EcFrmR and combined with biochemical/biophysical data suggests a mechanistic model for formaldehyde-sensing and derepression of frmRA(B) expression in numerous bacterial species.
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|Publisher Web site:||https://doi.org/10.1038/srep38879|
|Publisher statement:||This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/|
|Date accepted:||15 November 2016|
|Date deposited:||12 December 2016|
|Date of first online publication:||09 December 2016|
|Date first made open access:||12 December 2016|
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