1990
DOI: 10.1128/jb.172.8.4587-4592.1990
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Actinobacillus pleuropneumoniae hlyX gene homology with the fnr gene of Escherichia coli

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Cited by 57 publications
(49 citation statements)
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References 37 publications
(13 reference statements)
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“…3). (43,62), and 28% identity to E. coli Fnr (47,57) and A. pleuropneumoniae HlyX (29). The highest homologies among these proteins were found in the helix-turn-helix motif in the C-terminal region (Fig.…”
Section: Resultsmentioning
confidence: 85%
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“…3). (43,62), and 28% identity to E. coli Fnr (47,57) and A. pleuropneumoniae HlyX (29). The highest homologies among these proteins were found in the helix-turn-helix motif in the C-terminal region (Fig.…”
Section: Resultsmentioning
confidence: 85%
“…4), as well as in the ORF240 (FnrN) protein of R. leguminosarum (6), whereas the N-terminal regions of the R. meliloti and A. caulinodans FixK proteins contained no cysteine residues. In A. pleuropneumoniae HlyX and P. aeruginosa Anr, the spacing between the cysteine residues was the same as in the Fnr protein (29,43,62). Expression of B. japonicum fixK is controlled by the FixlJ system.…”
Section: Resultsmentioning
confidence: 99%
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“…Expression of a heterologous fnr gene (the hlyX gene of Actinobacillus pleuropneumoniae) confers a haemolytic phenotype upon E. coli K-12 (Lian et al, 1989;Green et al, 1992). The primary structure of HlyX is 73% identical to that of FNR (MacInnes et al, 1990). Like FNR, HlyX senses and responds to oxygen through the assembly/ disassembly of a [4Fe-4S] 2þ cluster and they recognize the same DNA target (Green and Baldwin, 1997a).…”
Section: Introductionmentioning
confidence: 99%
“…For example, Escherichia coli Fnr (fumarate-nitrate reduction regulator) mediates global changes in gene expression during transitions between aerobic and anaerobic growth (12). Fnr homologs have been described for a number of bacterial species (7,16,22,29), including Shewanella oneidensis MR-1 (20) (formerly Shewanella putrefaciens MR-1 [28]), a facultatively anaerobic metal-reducing bacterium (19). The predicted S. oneidensis EtrA (electron transport regulator) protein (20) shares a high degree of amino acid sequence identity with E. coli Fnr and with the analogous Anr (anaerobic regulator of arginine deiminase and nitrate reductase) protein from Pseudomonas aeruginosa (50.8 and 73.6% identity, respectively), thus suggesting the possibility that etrA is involved in regulating anaerobic energy metabolism in MR-1 (20).…”
mentioning
confidence: 99%