Promoter analysis of the catalase-peroxidase gene (<i>cpeA</i>) from<i>Rhodobacter capsulatus</i>

Forkl, Hubert; Drews, Gerhart; Tadros, Monier H.

doi:10.1111/j.1574-6968.1996.tb08101.x

FEMS Microbiology Letters

1996

DOI: 10.1111/j.1574-6968.1996.tb08101.x

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Promoter analysis of the catalase-peroxidase gene (cpeA) fromRhodobacter capsulatus

Hubert Forkl

Gerhart Drews

Monier H. Tadros

Abstract: The expression of the Rhodobacter capsulatus catalase-peroxidase (cpeA) was studied by in-frame fusions of the upstream region of the cpeA gene to a promoter-less lacZ gene. The transcription of the cpeA gene is about 20-50-fold higher under aerobic-dark than under anaerobic-light conditions. The promoter was localized within a 69-bp upstream DNA region. The transcription start site, determined by primer extension, is 28 bases upstream from the initiation codon, confirming the postulated promoter localized by … Show more

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Cited by 4 publications

References 16 publications

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Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Zeilstra-Ryalls

Kaplan²

2004

Cellular and Molecular Life Sciences (CMLS)

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The means by which oxygen intervenes in gene expression has been examined in considerable detail in the metabolically versatile bacterium Rhodobacter sphaeroides. Three regulatory systems are now known in this organism, which are used singly and in combination to modulate genes in response to changing oxygen availability. The outcome of these regulatory events is that the molecular machinery is present for the cell to obtain energy by means that are best suited to prevailing conditions, while at the same time maintaining cellular redox balance. Here, we explore the dangers associated with molecular oxygen relative to the various metabolisms used by R. sphaeroides, and then present the most recent findings regarding the features and operation of each of the three regulatory systems which collectively mediate oxygen control in this organism.

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Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Zeilstra-Ryalls

Kaplan²

2004

Cellular and Molecular Life Sciences (CMLS)

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Cloning and Expression of the Catalase Gene from the Anaerobic Bacterium Desulfovibrio vulgaris (Miyazaki F)

Kitamura

Nakanishi

Kojima

et al. 2001

Journal of Biochemistry

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We identified a gene encoding a catalase from the anaerobic bacteria Desulfovibrio vulgaris (Miyazaki F), and the expression of its gene in Escherichia coli. The 3.3-kbp DNA fragment isolated from D. vulgaris (Miyazaki F) by double digestion with EcoRI and SalI was found to produce a protein that binds protoheme IX as a prosthetic group in E. coli. This DNA fragment contained a putative open reading frame (Kat) and one part of another open reading frame (ORF-1). The amino acid sequence of the amino terminus of the protein purified from the transformed cells was consistent with that deduced from the nucleotide sequence of Kat in the cloned fragment of D. vulgaris (Miyazaki F) DNA, which may include promoter and regulatory sequences. The nucleotide sequence of Kat indicates that the protein is composed of 479 amino acids per monomer. The recombinant catalase was found to be active in the decomposition of hydrogen peroxide, as are other catalases from aerobic organisms, but its K(m) value was much greater. The hydrogen peroxide stress against D. vulgaris (Miyazaki F) induced the activity for the decomposition of hydrogen peroxide somewhat, so the catalase gene may not work effectively in vivo.

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Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

Bandyopadhyay

Steinman

2000

J Bacteriol

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Legionella pneumophila, the causative organism of Legionnaires' pneumonia, contains two enzymes with catalatic and peroxidatic activity, KatA and KatB. To address the issue of redundant, overlapping, or discrete in vivo functions of highly homologous catalase-peroxidases, the gene for katA was cloned and its function was studied in L. pneumophila and Escherichia coli and compared with prior studies of katB in this laboratory. katA is induced during exponential growth and is the predominant peroxidase in stationary phase. When katA is inactivated, L. pneumophila is more sensitive to exogenous hydrogen peroxide and less virulent in the THP-1 macrophage cell line, similar to katB. Catalatic-peroxidatic activity with different peroxidatic cosubstrates is comparable for KatA and KatB, but KatA is five times more active towards dianisidine. In contrast with these examples of redundant or overlapping function, stationary-phase survival is decreased by 100-to 10,000-fold when katA is inactivated, while no change from wild type is seen for the katB null. The principal clue for understanding this discrete in vivo function was the demonstration that KatA is periplasmic and KatB is cytosolic. This stationary-phase phenotype suggests that targets sensitive to hydrogen peroxide are present outside the cytosol in stationary phase or that the peroxidatic activity of KatA is critical for stationary-phase redox reactions in the periplasm, perhaps disulfide bond formation. Since starvation-induced stationary phase is a prerequisite to acquisition of virulence by L. pneumophila, further studies on the function and regulation of katA in stationary phase may give insights on the mechanisms of infectivity of this pathogen.

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Promoter analysis of the catalase-peroxidase gene (cpeA) fromRhodobacter capsulatus

Cited by 4 publications

References 16 publications

Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Cloning and Expression of the Catalase Gene from the Anaerobic Bacterium Desulfovibrio vulgaris (Miyazaki F)

Catalase-Peroxidases of Legionella pneumophila : Cloning of the katA Gene and Studies of KatA Function

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