A role for iron in transcriptional activation by FNR
- 23 August 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 329 (1-2), 55-58
- https://doi.org/10.1016/0014-5793(93)80192-w
Abstract
FNR is a transcriptional regulator which controls the expression of target genes in response to anoxia in Escherichia coli. The mechanism by which FNR senses and responds to anaerobiosis is unknown but indirect evidence suggests that an iron cofactor is involved. Using KMnO4 as a probe for DNA melting at active promoters, footprinting studies have now shown that the ferrous iron chelator, ferrozine, inhibits open complex formation in vivo, and that FNR with a high iron-content is essential for open complex formation in vitro. Since open complex formation is an essential pre-requisite for transcription, it is concluded that transcriptional activation by FNR is mediated by a ferrous iron cofactor.Keywords
This publication has 15 references indexed in Scilit:
- Properties of FNR proteins substituted at each of the five cysteine residuesMolecular Microbiology, 1993
- FNR activates and represses transcription in vitroProceedings Of The Royal Society B-Biological Sciences, 1991
- Characterization of the FNR protein of Escherichia coli , an iron-binding transcriptional regulatorProceedings Of The Royal Society B-Biological Sciences, 1991
- Oxygen regulated gene expression in Escherichia coli: Control of anaerobic respiration by the FNR proteinAntonie van Leeuwenhoek, 1991
- Activator-dependent preinduction binding of .sigma.-70 RNA polymerase at the metal-regulated mer promoterBiochemistry, 1990
- In vivo and in vitro mutants of FNR the anaerobic transcriptional regulator of E.coliFEBS Letters, 1990
- FNR and its role in oxygen-regulated gene expression inEscherichia coliFEMS Microbiology Letters, 1990
- Effect of positive redox potentials (>+400mV) on the expression of anaerobic respiratory enzymes in Escherichia coliMolecular Microbiology, 1990
- Cloning of binding sequences for theEscherichia colitranscription activators, FNR and CRP: location of bases involved in discrimination between FNR and CRPNucleic Acids Research, 1989
- Inactivation of the FNR protein of Escherichia coli by targeted mutagenesis in the N‐terminal regionMolecular Microbiology, 1988