Binding to DNA Protects Neisseria meningitidis Fumarate and Nitrate Reductase Regulator (FNR) from Oxygen

Edwards, James, Cole, Lindsay J, Green, Jasper B, Thomson, Melanie J, Wood, A Jamie, Whittingham, Jean L and Moir, James W B 2010, Binding to DNA Protects Neisseria meningitidis Fumarate and Nitrate Reductase Regulator (FNR) from Oxygen, Journal of Biological Chemistry, vol. 285, no. 2, pp. 1105-1112, doi: 10.1074/jbc.M109.057810.

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Title Binding to DNA Protects Neisseria meningitidis Fumarate and Nitrate Reductase Regulator (FNR) from Oxygen
Author(s) Edwards, James
Cole, Lindsay J
Green, Jasper B
Thomson, Melanie J
Wood, A Jamie
Whittingham, Jean L
Moir, James W B
Journal name Journal of Biological Chemistry
Volume number 285
Issue number 2
Start page 1105
End page 1112
Total pages 8
Publisher American Society for Biochemistry and Molecular Biology Inc.
Place of publication Rockville, Md.
Publication date 2010
ISSN 0021-9258
Keyword(s) Cytochromes
Extracellular matrix proteins
Ligand binding protein
Myeloid cell
Summary Here, we report the overexpression, purification, and characterization of the transcriptional activator fumarate and nitrate reductase regulator from the pathogenic bacterium Neisseria meningitidis (NmFNR). Like its homologue from Escherichia coli (EcFNR), NmFNR binds a 4Fe-4S cluster, which breaks down in the presence of oxygen to a 2Fe-2S cluster and subsequently to apo-FNR. The kinetics of NmFNR cluster disassembly in the presence of oxygen are 2–3× slower than those previously reported for wild-type EcFNR, but similar to constitutively active EcFNR* mutants, consistent with earlier work in which we reported that the activity of FNR-dependent promoters in N. meningitidis is only weakly inhibited by the presence of oxygen (Rock, J. D., Thomson, M. J., Read, R. C., and Moir, J. W. (2007) J. Bacteriol. 189, 1138–1144). NmFNR binds to DNA containing a consensus FNR box sequence, and this binding stabilizes the iron-sulfur cluster in the presence of oxygen. Partial degradation of the 4Fe-4S cluster to a 3Fe-4S occurs, and this form remains bound to the DNA. The 3Fe-4S cluster is converted spontaneously back to a 4Fe-4S cluster under subsequent anaerobic reducing conditions in the presence of ferrous iron. The finding that binding to DNA stabilizes FNR in the presence of oxygen such that it has a half-life of ∼30 min on the DNA has implications for our appreciation of how oxygen switches off FNR activatable genes in vivo.
Language eng
DOI 10.1074/jbc.M109.057810
Field of Research 110309 Infectious Diseases
110303 Clinical Microbiology
Socio Economic Objective 970111 Expanding Knowledge in the Medical and Health Sciences
HERDC Research category C1.1 Refereed article in a scholarly journal
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Document type: Journal Article
Collections: Faculty of Health
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