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D-Glutamate Utilization in Pseudomonas aeruginosa PAO1

ABSTRACT: D-Glutamate (D-Glu), an essential component of peptidoglycans, can be utilized as carbon and nitrogen source by Pseudomonas aeruginosa. DNA microarrays were employed to identify genes involved in D-Glu catabolism. Through gene knockout and growth phenotype analysis, the divergent dguR-dguABC (D-glutamate utilization) gene cluster was shown to participate in D-Glu catabolism and regulation. The dguA gene encodes a FAD-dependent D-amino acid dehydrogenase with D-Glu as its preferred substrate, and its promoter was specifically induced by exogenous D-Glu and D-Gln. The function of DguR as transcriptional activator of the dguABC operon was demonstrated by promoter activity measurements in vivo and by mobility shift assays with purified His-tagged DguR in vitro. Although the DNA-binding activity of DguR did not require D-Glu, the presence of D-Glu in the binding reaction was found to stabilize a preferred nucleoprotein complex. The dguB gene encodes a putative enamine/imine deaminase of the RidA family, but its role in D-Glu catabolism remained to be determined. While a lesion in dguC encoding a periplasmic solute binding protein did not affect growth on D-Glu, the AatJMQP transporter for acidic amino acid uptake was found essential for D-Glu and L-Glu utilization. Expression of this uptake system was subjected to induction by exogenous DL-Glu, most likely via the AauSR two-component system. In summary, DguA was identified in this study as a new member of the FAD-dependent amino acid dehydrogenase family for D-amino acid catabolism. DguR serves as a D-Glu sensor and transcriptional activator of the dguA promoter.

ORGANISM(S): Pseudomonas aeruginosa Pseudomonas aeruginosa PAO1

PROVIDER: GSE46603 | GEO | 2013/05/03

SECONDARY ACCESSION(S): PRJNA201067

REPOSITORIES: GEO

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D-Glutamate Utilization in Pseudomonas aeruginosa PAO1

Project description:D-Glutamate (D-Glu), an essential component of peptidoglycans, can be utilized as carbon and nitrogen source by Pseudomonas aeruginosa. DNA microarrays were employed to identify genes involved in D-Glu catabolism. Through gene knockout and growth phenotype analysis, the divergent dguR-dguABC (D-glutamate utilization) gene cluster was shown to participate in D-Glu catabolism and regulation. The dguA gene encodes a FAD-dependent D-amino acid dehydrogenase with D-Glu as its preferred substrate, and its promoter was specifically induced by exogenous D-Glu and D-Gln. The function of DguR as transcriptional activator of the dguABC operon was demonstrated by promoter activity measurements in vivo and by mobility shift assays with purified His-tagged DguR in vitro. Although the DNA-binding activity of DguR did not require D-Glu, the presence of D-Glu in the binding reaction was found to stabilize a preferred nucleoprotein complex. The dguB gene encodes a putative enamine/imine deaminase of the RidA family, but its role in D-Glu catabolism remained to be determined. While a lesion in dguC encoding a periplasmic solute binding protein did not affect growth on D-Glu, the AatJMQP transporter for acidic amino acid uptake was found essential for D-Glu and L-Glu utilization. Expression of this uptake system was subjected to induction by exogenous DL-Glu, most likely via the AauSR two-component system. In summary, DguA was identified in this study as a new member of the FAD-dependent amino acid dehydrogenase family for D-amino acid catabolism. DguR serves as a D-Glu sensor and transcriptional activator of the dguA promoter. Pseudomonas aeruginosa PAO1 was chosen as model to study gene response with different D-amino acids.

2013-05-03 | E-GEOD-46603 | biostudies-arrayexpress

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Project description:P. aeruginosa possesses the ability to utilize a wild range of compounds as the sole source of carbon and nitrogen, including proteogenic amino acids. In particular, utilization of L-Asp and L-Asn is insensitive to carbon catabolite repression as strong growth retains in the cbrAB mutants devoid of the essential regulators for the activation of most catabolic genes. Transcriptome analysis and functional characterization were conducted to identify genes that participate in the catabolism, uptake, and regulation of these two amino acids. Through gene knockout and growth phenotype analysis, degradation of L-Asn to L-Asp was shown to be mediated by two asparaginases AsnA and AsnB, whereas only AnsB is required for the deamidation of D-Asn to D-Asp. While D-Asp is a dead-end product, conversion of L-Asp to fumurate is catalyzed by an aspartase AspA as further evidenced by enzyme kinetics. The results from the measurements of promoter-lacZ expression in vivo and mobility shift assays in vitro demonstrated that the asnR and aspR genes encode two transcriptional regulators in response to L-Asn and L-Asp, respectively, for the induction of the ansPA operon and the aspA gene. In addition, exogenous L-Glu also cause induction of the aspA gene, most likely due to its conversion to L-Asp by the aspartate transaminase AspC. Expression of several transporters were also found inducible by L-Asn and/or L-Asp, including AatJQMP for acid amino acids, DctA and DctPQM for C4-dicarboxylates, and PA5530 for C5-dicarboxylates. In summary, a complete pathway and regulation for L-Asn and L-Asp catabolism was established in this study. Cross induction of three transport systems for dicarboxylic acids may provide a physiological explanation for the insensitivity of L-Asn and L-Asp utilization to carbon catabolite repression.

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