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A 12-cistron Escherichia coli operon (hyf) encoding a putative proton-translocating formate hydrogenlyase system.
It is proposed that Hyf, in conjunction with formate dehydrogenase H (Fdh-H), forms a hitherto unrecognized respiration-linked proton-translocating formate hydrogenlyase (FHL-2) that is likely to act as a formate-dependent regulator of the hyf operon and that FocB provides the Hyf complex with external formate as substrate. Expand
FNR and its role in oxygen-regulated gene expression in Escherichia coli.
The purpose of this review is to summarize what is known about FNR, the transcriptional regulator which is essential for expressing anaerobic respiratory processes in E. coli. Expand
Ferritin Mutants of Escherichia coli Are Iron Deficient and Growth Impaired, and fur Mutants are Iron Deficient
- Hossein Abdul-Tehrani, A. Hudson, +6 authors S. Andrews
- Biology, Medicine
- Journal of bacteriology
- 1 March 1999
It is concluded that FtnA acts as an iron store accommodating up to 50% of the cellular iron during postexponential growth in iron-rich media and providing a source of iron that partially compensates for iron deficiency during iron-restricted growth. Expand
Reconstitution of the [4Fe-4S] cluster in FNR and demonstration of the aerobic-anaerobic transcription switch in vitro.
- J. Green, B. Bennett, P. Jordan, E. Ralph, A. Thomson, J. Guest
- Biology, Medicine
- The Biochemical journal
- 15 June 1996
The FNR protein of Escherichia coli is a redox-responsive transcription regulator that activates and represses a family of genes required for anaerobic and aerobic metabolism and its inactivation under aerobic conditions provides a demonstration in vitro of the FNR-mediated aerobic-anaerobic transcriptional switch. Expand
Functional versatility in the CRP-FNR superfamily of transcription factors: FNR and FLP.
The cAMP receptor protein and the fumarate and nitrate reduction regulator of Escherichia coli are founder members of an expanding superfamily of structurally related transcription factors, and the basic structural fold has been adapted in FNR and FLP by the acquisition in the N-terminal region of different combinations of cysteine or other residues. Expand
A new family of bacterial regulatory proteins.
A helix-turn-helix motif is predicted in the most highly-conserved segment of each protein suggesting that they are members of a new family of helix/turn/helix DNA-binding proteins. Expand
Catabolism of L-lysine by Pseudomonas aeruginosa.
The results suggested that the growth rate of the parental strain is limited by the rate of transport and/or decarboxylation of L-lysine, and the cadaverine pathway was present, but not so highly induced, in the parent strain P. aeruginosa PACI. Expand
Transcriptional regulation and organization of the dcuA and dcuB genes, encoding homologous anaerobic C4-dicarboxylate transporters in Escherichia coli.
The results show that dcuA is constitutively expressed whereas dcuB expression is highly regulated, which is entirely consistent with a primary role for DcuB in mediating C4-dicarboxylate transport during anaerobic fumarate respiration. Expand
The FNR Modulon and FNR-Regulated Gene Expression
A major current challenge is to understand how multiple regulatory factors exert their various effects on a single transcriptional unit, and whether such interactions are sufficient to establish and maintain the complex coordinated metabolic networks operating under diverse physiological conditions. Expand
FNR and its role in oxygen-regulated gene expression in Escherichia coli
It is clear that oxygen functions as a regulatory signal controlling several important aspects of mitcrobial physiology, and further studies should reveal the molecular basis of the mechanism by which changes in oxygen tension are sensed. Expand