Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12

Oliver, G.; Gosset, Guillermo; Sánchez-Pescador, Ray; Lozoya, Edmundo; Ku, Lailig M.; Flores, Noemí; Becerril, Baltazar; Valle, Fernando; Bolívar, Francisco

doi:10.1016/0378-1119(87)90207-1

Cited by 89 publications

(76 citation statements)

References 36 publications

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“…2a indicated that the first 14 residues of the translated GltB sequence are absent and that the purified GltB protein has a terminal cysteine residue, which normally cannot be detected by a protein sequencer. Similar aminoterminal processing of GltB has been reported for E. coli (25). In the case of GltD, comparison of the derived sequence to the determined sequence indicated that the first methionine residue of GltD was removed.…”

Section: Resultssupporting

confidence: 72%

“…The molecular mass of GltBD of P. aeruginosa was estimated by molecular sieving to be 230 kDa, indicating that the native enzyme is a single heterodimer. In contrast, the native GltBD protein of E. coli selfassociates into a tetrameric form (25). Furthermore, unpublished work done in this laboratory showed that GltBD of E. coli did not bind to heparin or to DNA, unlike GltBD of P. aeruginosa, which binds to heparin (this study) and has been found earlier to bind certain DNA fragments (16).…”

Section: Resultsmentioning

confidence: 52%

“…The open reading frames of the gltB and gltD genes have coding capacities for polypeptides of 161.6 and 52.6 kDa, respectively. The derived amino acid sequences of GltB and GltD of PAO1 exhibit 75 and 80% sequence similarity (data not shown), respectively, to the large and small subunits of GOGAT of E. coli (25). The gltBD operon of PAO1 is separated by two putative rhoindependent terminators from an upstream PA5037 gene, which encodes a hypothetical protein, and from the downstream hemE gene, which encodes uroporphyrinogen decarboxylase (PAO1 genome annotation project; www.pseudomonas.com).…”

Section: Resultsmentioning

confidence: 99%

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The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

et al. 2004

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The arginine regulatory protein of Pseudomonas aeruginosa, ArgR, is essential for induction of operons that encode enzymes of the arginine succinyltransferase (AST) pathway, which is the primary route for arginine utilization by this organism under aerobic conditions. ArgR also induces the operon that encodes a catabolic NAD ؉ -dependent glutamate dehydrogenase (GDH), which converts L-glutamate, the product of the AST pathway, in ␣-ketoglutarate. The studies reported here show that ArgR also participates in the regulation of other enzymes of glutamate metabolism. Exogenous arginine repressed the specific activities of glutamate synthase (GltBD) and anabolic NADP-dependent GDH (GdhA) in cell extracts of strain PAO1, and this repression was abolished in an argR mutant. The promoter regions of the gltBD operon, which encodes GltBD, and the gdhA gene, which encodes GdhA, were identified by primer extension experiments. Measurements of ␤-galactosidase expression from gltB::lacZ and gdhA::lacZ translational fusions confirmed the role of ArgR in mediating arginine repression. Gel retardation assays demonstrated the binding of homogeneous ArgR to DNA fragments carrying the regulatory regions for the gltBD and gdhA genes. DNase I footprinting experiments showed that ArgR protects DNA sequences in the control regions for these genes that are homologous to the consensus sequence of the ArgR binding site. In silica analysis of genomic information for P. fluorescens, P. putida, and P. stutzeri suggests that the findings reported here regarding ArgR regulation of operons that encode enzymes of glutamate biosynthesis in P. aeruginosa likely apply to other pseudomonads.The arginine succinyltransferase (AST) pathway (Fig. 1) is the major route for arginine catabolism under aerobic conditions in Pseudomonas aeruginosa, This pathway converts Larginine into L-glutamate with the concomitant release of three nitrogen moieties (11,13,14). Utilization of arginine as a carbon source entails deamination of glutamate to ␣-ketoglutarate, which is then channeled into the tricarboxylic acid (TCA) cycle. We have recently reported (18) the cloning and characterization of gdhB, which encodes a novel NAD ϩ -dependent glutamate dehydrogenase (NAD-GDH; GdhB). The expression of gdhB was shown to be inducible by exogenous arginine, and this induction was mediated by ArgR, the arginine regulatory protein. The activity of GdhB, a tetramer of equal 180-kDa subunits, was also found to be subject to allosteric activation by arginine. The induction of gdhB expression and the activation by arginine of the encoded enzyme clearly serve as mechanisms that coordinate aerobic utilization of arginine as a carbon source with glutamate utilization via the TCA cycle.The ArgR protein of P. aeruginosa does not exhibit any sequence homology to the arginine regulatory proteins from enteric bacteria (17,19) or Bacillus subtilis (5). Rather, ArgR of P. aeruginosa is a member of the AraC/XylS family of transcriptional regulators (27) and functions like other members of th...

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Section: Resultssupporting

confidence: 72%

Section: Resultsmentioning

confidence: 52%

Section: Resultsmentioning

confidence: 99%

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The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

et al. 2004

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“…Each primer is complementary to conserved sequences in the Fd-GOGAT of tobacco (Zehnacker et al, 1992) and barley (Avila et al, 1993) and the NADH-GOGAT of alfalfa (Gregerson et al, 1993b) and Escherichia coli (Oliver et al, 1987) (see Fig. 1).…”

Section: Pcr For Nadh-gogatmentioning

confidence: 99%

“…To determine if there are other NADH-GOGAT isoforms in alfalfa, we designed degenerate primers from the conserved regions of the deduced amino acid sequence of Fd-GOGAT from tobacco (Zehnacker et al, 1992) and barley (Avila et al, 1993) and the NADH-GOGAT from alfalfa (Gregerson et al, 1993b) and E. coli (Oliver et al, 1987) (Fig. 1).…”

Section: Screening For Other Nadh-gogat Isoforms In the Alfalfa Genommentioning

confidence: 99%

NADH-Glutamate Synthase in Alfalfa Root Nodules. Genetic Regulation and Cellular Expression1

et al. 1999

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Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase

Filetici

Martegani

Valenzuela

et al. 1996

Yeast

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Determination of the nucleotide sequence for the glutamate synthase structural genes of Escherichia coli K-12

Cited by 89 publications

References 36 publications

The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

The Arginine Regulatory Protein Mediates Repression by Arginine of the Operons Encoding Glutamate Synthase and Anabolic Glutamate Dehydrogenase in Pseudomonas aeruginosa

NADH-Glutamate Synthase in Alfalfa Root Nodules. Genetic Regulation and Cellular Expression1

Sequence of the GLT1 gene from Saccharomyces cerevisiae reveals the domain structure of yeast glutamate synthase

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