The Escherichia coli FNR protein is an oxygen-responsive global transcription factor, and OxyR is a key regulator of the peroxide stress response. Here both FNR and OxyR are shown to regulate expression of the E. coli yhjA gene. The yhjA gene encodes a predicted cytochrome c peroxidase, a bacterial haem-containing protein involved in the peroxide stress response through its ability to convert hydrogen peroxide to water. It is shown that the yhjA gene of E. coli possesses a class II FNR site and an OxyR site upstream of the yhjA transcript start. Expression of yhjA was found to be dependent on this unusual combination of FNR and OxyR under conditions of oxygen starvation. Phenotypic analysis of the yhjA mutant revealed increased sensitivity to exogenous hydrogen peroxide and organic peroxides during growth under anaerobic conditions, consistent with the observed regulation and predicted function of the yhjA gene product.
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http://dx.doi.org/10.1099/mic.0.2006/004838-0 | DOI Listing |
Biochim Biophys Acta Bioenerg
June 2018
Microbial Stress Lab, UCIBIO, REQUIMTE, Departamento de Química, Faculdade de Ciências e Tecnologia, Universidade Nova de Lisboa, Campus da Caparica, 2829-516 Caparica, Portugal. Electronic address:
The trihemic bacterial cytochrome c peroxidase from Escherichia coli, YhjA, is a membrane-anchored protein with a C-terminal domain homologous to the classical bacterial peroxidases and an additional N-terminal (NT) heme binding domain. Recombinant YhjA is a 50 kDa monomer in solution with three c-type hemes covalently bound. Here is reported the first biochemical and spectroscopic characterization of YhjA and of the NT domain demonstrating that NT heme is His63/Met125 coordinated.
View Article and Find Full Text PDFProc Natl Acad Sci U S A
August 2017
Department of Microbiology, University of Illinois, Urbana, IL 61801
Microbial cytochrome peroxidases (Ccp) have been studied for 75 years, but their physiological roles are unclear. Ccps are located in the periplasms of bacteria and the mitochondrial intermembrane spaces of fungi. In this study, Ccp is demonstrated to be a significant degrader of hydrogen peroxide in anoxic Intriguingly, transcription requires both the presence of HO and the absence of O Experiments show that Ccp lacks enough activity to shield the cytoplasm from exogenous HO However, it receives electrons from the quinone pool, and its flux rate approximates flow to other anaerobic electron acceptors.
View Article and Find Full Text PDFBioleaching processes are used to recover metals from sulfidic ores. Biofilm formation on ores is important for bioleaching because the attached microorganisms start the leaching process by concentrating ferric ions in the extracellular matrix. It has been shown that hydrogen peroxide is spontaneously generated on the surface of ores and that it negatively influences the growth and activity of microorganisms.
View Article and Find Full Text PDFMicrobiology (Reading)
May 2007
Department of Molecular Biology and Biotechnology, The University of Sheffield, Sheffield S10 2TN, UK.
The Escherichia coli FNR protein is an oxygen-responsive global transcription factor, and OxyR is a key regulator of the peroxide stress response. Here both FNR and OxyR are shown to regulate expression of the E. coli yhjA gene.
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