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The mechanism of a formaldehyde-sensing transcriptional regulator

Denby, K.J.; Iwig, J.; Bisson, C.; Westwood, J.; Rolfe, M.D.; Sedelnikova, S.E.; Higgins, K.; Maroney, M.J.; Baker, P.J.; Chivers, P.T.; Green, J.

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K.J. Denby

J. Iwig

C. Bisson

J. Westwood

M.D. Rolfe

S.E. Sedelnikova

K. Higgins

M.J. Maroney

P.J. Baker

J. Green


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.


Denby, K., Iwig, J., Bisson, C., Westwood, J., Rolfe, M., Sedelnikova, S., …Green, J. (2016). The mechanism of a formaldehyde-sensing transcriptional regulator. Scientific Reports, 6, Article 38879.

Journal Article Type Article
Acceptance Date Nov 15, 2016
Online Publication Date Dec 9, 2016
Publication Date Dec 9, 2016
Deposit Date Dec 9, 2016
Publicly Available Date Dec 12, 2016
Journal Scientific Reports
Publisher Nature Research
Peer Reviewed Peer Reviewed
Volume 6
Article Number 38879


Published Journal Article (1.7 Mb)

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