Comparative analysis of the cya locus in enterobacteria and related Gram-negative facultative anaerobes

Trotot, Pascale; Sismeiro, Odile; Vivarès, Christian P.; Glaser, Philippe; Bresson-Roy, A.; Danchin, Antoine

doi:10.1016/0300-9084(96)82192-4

Cited by 15 publications

(12 citation statements)

References 26 publications

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“…There are numerous reports of hem gene clusters, and hemCD operons are especially common (1,19,23,29,46). However, no other cases of clustering of hemC and hemE were found in a search of the GenBank database.…”

Section: Discussionmentioning

confidence: 99%

Oxygen-Mediated Regulation of Porphobilinogen Formation inRhodobacter capsulatus

et al. 2002

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A Rhodobacter capsulatus hemC mutant has been isolated and used to show that oxygen regulates the intracellular levels of porphobilinogen. Experiments using a hemB-cat gene fusion demonstrated that oxygen does not transcriptionally regulate hemB transcription. Porphobilinogen synthase activity is not regulated by oxygen nor is the enzyme feedback inhibited by hemin or protoporphyrin IX. It was demonstrated that less than 20% of [ 14 C]aminolevulinate was incorporated into bacteriochlorophyll, suggesting that the majority of the aminolevulinate is diverted from the common tetrapyrrole pathway. Porphobilinogen oxygenase activity was not observed in this organism; however, an NADPH-linked aminolevulinate dehydrogenase activity was demonstrated. The specific activity of this enzyme increased with increasing oxygen tension. The results presented here suggest that carbon flow over the common tetrapyrrole pathway is regulated by a combination of feedback inhibition of aminolevulinate synthase and diversion of aminolevulinate from the pathway by aminolevulinate dehydrogenase.

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Section: Discussionmentioning

confidence: 99%

Oxygen-Mediated Regulation of Porphobilinogen Formation inRhodobacter capsulatus

et al. 2002

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“…Recipient strains were screened for the restoration of YplA activity on PLA indicator medium. Cosmids that restored YplA activity were identified, and one was used as a template to amplify the cya region using oligonucleotide primers (GYcya1, 5Ј-GCT TGC CAT AAG GCG AG-3Ј, and GYcya2, 5Ј-TAC ATC AGG TAT GGC-3Ј) based on the sequence of cya from Yersinia intermedia (32). DNA amplification, subsequent cloning, and subcloning were conducted by procedures described above for crp.…”

Section: Methodsmentioning

confidence: 99%

Essential Role for Cyclic AMP and Its Receptor Protein in Yersinia enterocolitica Virulence

Petersen

Young

2002

Infect Immun

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Insertion mutations were isolated in cya and crp of Yersinia enterocolitica, which encode adenylate cyclase and the cyclic AMP (cAMP) receptor protein (CRP). The cya and crp mutants were affected for the production of proteins exported by the Ysc, Ysa, and flagellar type III secretion systems (TTSS). Protein production by each TTSS was restored when the respective mutation was complemented by a plasmid-encoded copy of the wild-type gene. Both cya and crp mutants exhibited reduced virulence for orally infected BALB/c mice in a 50% lethal dose analysis. Examination of bacterial survival in host tissues showed that cya and crp mutants colonized Peyer's patches and, to a lesser extent, mesenteric lymph nodes. However, the mutants did not appear to disseminate to the liver and spleen of infected mice. An initial examination of the effectiveness of Y. enterocolitica cya and crp mutants to stimulate protective immunity against subsequent challenge with virulent bacteria in mice was promising. The results indicate that the cAMP-CRP regulatory system is required for Y. enterocolitica virulence.

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“…1). In enterobacteria, the cyaY gene is localized near the gene encoding adenylyl cyclase ( cya ), hence its name, before the downstream dapF gene [11]. Its open reading frame (ORF) is in the complementary strand with respect to cya .…”

Section: Introductionmentioning

confidence: 99%

Knock‐out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants

Ohshima

Jiralerspong

et al. 1999

FEBS Letters

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Friedreich ataxia is a recessively inherited neurodegenerative disease caused by deficiency of a highly conserved mitochondrial protein, frataxin. Frataxin deficiency results in mitochondrial iron accumulation and oxidative stress. Frataxin shows homology with the CyaY proteins of Q Q-purple bacteria, whose function is unknown. We knocked out the CyaY gene in Escherichia coli MM383 by homologous recombination and we generated an E. coli MM383 strain overexpressing CyaY. Bacterial growth, iron content and survival after exposure to H 2 O 2 did not differ among these strains, suggesting that, despite structural similarities, cyaY proteins in bacteria may have a different function from frataxin homologues in mitochondria.z 1999 Federation of European Biochemical Societies.

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Comparative analysis of the cya locus in enterobacteria and related Gram-negative facultative anaerobes

Cited by 15 publications

References 26 publications

Oxygen-Mediated Regulation of Porphobilinogen Formation inRhodobacter capsulatus

Oxygen-Mediated Regulation of Porphobilinogen Formation inRhodobacter capsulatus

Essential Role for Cyclic AMP and Its Receptor Protein in Yersinia enterocolitica Virulence

Knock‐out of the cyaY gene in Escherichia coli does not affect cellular iron content and sensitivity to oxidants

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