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Matsushika A, Mizuno T: A dual-signalling mechanism mediated by the ArcB hybrid sensor kinase containing the histidine-containing phosphotransfer domain in Escherichia coli. J Bacteriol 1998, 180:3973-3977. An amino acid exchange in the HPt domain of ArcB affected anaerobic repression by ArcA of the sdh operon. Nevertheless, the mutant ArcB protein retained signalling capacity for other genes. The conclusion is that ArcB has more than one signalling pathway.
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Dixon R: The oxygen-responsive NIFL-NIFA complex: A novel two component regulatory system controlling nitrogenase synthesis in γ-proteobacteria. Arch Microbiol 1998, 169:371-380. An excellent review describing details of the novel NIFL/NIFA two-component regulatory system that senses redox, energy and the fixed-nitrogen status of the cell. Comparisons are drawn between NIFL and other redox sensor proteins (e.g. Aer and FIXL).
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Taylor BL, Zhulin IB: In search of higher energy: Metabolism-dependent behaviour in bacteria. Mol Microbiol 1998, 28:683-690.
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Söderbäck E, Reyes-Ramirez F, Eydmann T, Austin S, Hill S, Dixon R: The redox- and fixed nitrogen-responsive regulatory protein, NIFL, from Azotobacter vinelandii is comprised of discrete flavin and nucleotide-binding domains. Mol Microbiol 1998, 28:179-192.
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Ingmer H, Miller CA, Cohen SN: Destabilized inheritance of pSc101 and other Escherichia coli plasmids by DpiA, a novel two-component system regulator. Mol Microbiol 1998, 29:49-59. This paper is seemingly unrelated to redox systems. Upon closer scrutiny, however, the authors uncover an interesting regulatory cascade in which the novel DpiAB two-component system regulates expression of appY, a transcriptional regulator of anaerobically expressed genes. The conclusion that can be drawn from this work is that the DpiA/DpiB proteins are involved directly or indirectly in redox-sensing. Potentially, they represent a component of a new redox-sensing system in E. coli.
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Colloms SD, Alén C, Sherratt DJ: The ArcA/ ArcB two-component regulatory system of Escherichia coli is essential for Xer site-specific recombination at psi. Mol Microbiol 1998, 28:521-530. This excellent paper demonstrates that ArcA has an ancillary, probably an architectural, function in site-specific recombination events involved in pSC101 replication. The implication from these studies is that plasmid replication is controlled in response to the redox status of the cell. There is also an interesting overlap with the findings of Ingmer et al. [24•].
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Nyström T: To be or not to be: The ultimate decision of the growth arrested cell. FEMS Microbiol Rev 1998, 21:283-290. This review discusses the role played by ArcA, along with other factors, in controlling bacterial ageing and stasis survival. What I particularly like in this review is that it bangs the drum for taking an holistic approach to studying bacteria.
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Nakano MM, Hulett FM: Adaptation of Bacillus subtilis to oxygen limitation. FEMS Lett 1997, 157:1-7. This paper reviews the cascade regulation underlying the control of adaptation in B. subtilis to anaerobiosis. This is a comparatively new field that poses many interesting questions for future study.
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Gostick DO, Green J, Irvine AS, Gasson MJ, Guest JR: A novel regulatory switch mediated by the FNR-like protein of Lactobacillus casei. Microbiology 1998, 144:705-717. This paper is full of interesting information concerning the FNR-like protein, FLP, of Lactobacillus casei. Diverse approaches are taken to study FLP and clear evidence is presented demonstrating that it is a redox-dependent transcriptional regulator, in which interconversion between transcriptionally active and inactive forms occurs by reversible disulphide bond formation. In this regard it is similar to OxyR of E. coli (see [40•]).
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Zheng M, Åslund F, Storz G: Activation of the OxyR transcription factor by reversible disulfide bond formation. Science 1998, 279:1718-1721. In contrast to earlier speculation, OxyR is shown to undergo a redox cycle of reversible disulphide bond formation. Oxidation occurs in response to exposure of the E. coli cell to hydrogen peroxide and reduction to the dithiol is controlled by glutaredoxin.
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Arai H, Kodama T, Igarashi Y: Cascade regulation of the two CRP/ FNR-related transcriptional regulators (ANR and DNR) and the denitrification enzymes in Pseudomonas aeruginosa. Mol Microbiol 1997, 25:1141-1148. This paper clarifies the cascade regulation observed for ANR and DNR. It demonstrates that the genes encoding denitrification enzymes are regulated directly by DNR, while ANR's involvement is indirect through the control of dnr expression. Other genes, in contrast, are shown to be regulated solely by ANR.
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Van Spanning RJM, De Boer APN, Reijnders WNM, Westerhoff HV, Stouthamer AH, Van Der Oost J: FnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitation. Mol Microbiol 1997, 23:893-907. By examining expression of the genes encoding various components of the respiratory chain in P. denitrificans the authors are able to propose a model in which FnrP is exclusively responsible for controlling synthesis of nitrate reductase and various oxidase components, while NNR exhibits exclusive control of nitrite and nitric oxide reductase synthesis. The paper also presents an interesting updated phylogenetic comparison of FNR-like proteins from various bacterial sources.
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