Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase

Bloom, Fredric R.; Levin, Marc S.; Foor, Forrest; Tyler, Bonnie

doi:10.1128/jb.134.2.569-577.1978

Cited by 55 publications

(18 citation statements)

References 27 publications

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“…G1nC mutants. Strains defective in glnD lack uridylyltransferase and uridylyl-removing enzyme (4,9). In E. coli, GlnD-strains have highly adenylylated GS under all conditions, fail to derepress GS under nitrogen-poor conditions, and grow poorly in the absence of glutamine (9).…”

Section: Resultsmentioning

confidence: 99%

“…In E. coli, GlnD-strains have highly adenylylated GS under all conditions, fail to derepress GS under nitrogen-poor conditions, and grow poorly in the absence of glutamine (9). Revertants with glnA-linked mutations which suppress the GlnDphenotype have been isolated, and they produce high levels of GS in the presence of ammonia, the GlnC phenotype (4,9).…”

Section: Resultsmentioning

confidence: 99%

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Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli

MacNeil¹,

MacNeil²,

Tyler³

1982

J Bacteriol

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A total of 399 independent mutants of Escherichia coli were obtained which have point and insertion mutations in the glnA region. Mutants isolated included Gln-and Reg-strains (unable to utilize arginine as a nitrogen source). Mutations were mapped with 73 deletion-containing derivatives of a A gln phage. Complementation analysis was performed with A gln derivatives containing point mutations which conferred a Gln-or Reg-phenotype. Deletion mapping and complementation analysis assigned 104 mutations in 24 deletion intervals to ginA. Mutations in Reg-strains were assigned to two genes, glnL and ginG. glnL contained 131 mutations in 12 deletion intervals, and gInG contained 164 mutations in 10 deletion intervals. The gene order is ginA-ginL-ginG, transcribed from left to right. Polarity ofinsertion mutations indicates that glnL and glnG form an operon. Complementation analysis of ginA insertion mutations with glnL and glnG mutations showed polarity of glnA onto most glnL and glnG alleles, suggesting that transcription of glnA may proceed into the ginL-glnG operon. All mutations analyzed in glnA conferred a Gln-phenotype. However, we also found that over half of the Glnstrains isolated after chemical mutagenesis contained point mutations in ginG. Mutants which synthesized a high level of glutamine synthetase in the presence of ammonia (GlnC phenotype) were selected as revertants of a strain with a TnlO insertion in glnD and were mapped with chromosomal deletions. Results indicate that mutations in 12 of 15 examined strains clearly map outside of ginA, probably in glnL.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli

MacNeil¹,

MacNeil²,

Tyler³

1982

J Bacteriol

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“…Like enteric bacteria, V. fischeri apparently co-ordinates N metabolism through the activity of the product of the glnD gene, which, if defective, leads to less efficient growth on amino acids (Table 2). However, unlike E. coli (Bloom et al, 1978), this defect of the glnD mutant is not relieved by the addition of glutamine in a minimal medium (Table 2). Nonetheless, a mixture of nitrogen sources such as that present in a tryptone-based medium does allow the V. fischeri glnD mutant to assume a wild-type growth rate.…”

Section: Discussionmentioning

confidence: 99%

Novel effects of a transposon insertion in the Vibrio fischeri glnD gene: defects in iron uptake and symbiotic persistence in addition to nitrogen utilization

Graf

Ruby²

2000

Molecular Microbiology

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Vibrio fischeri is the sole species colonizing the light‐emitting organ of the Hawaiian squid, Euprymna scolopes. Upon entering the nascent light organ of a newly hatched juvenile squid, the bacteria undergo morphological and physiological changes that include the loss of flagellation and the induction of bioluminescence. These and other events reveal a pattern of genetic regulation that is a response to the colonization of host tissue. In this study, we isolated and characterized a glnD::mTn5Cm mutant of V. fischeri. In addition to the predicted defects in the efficiency of nitrogen utilization, this glnD mutant had an unexpected reduction in the ability to produce siderophore and grow under iron‐limiting conditions. Although the glnD mutant could colonize juvenile squid normally over the first 24 h, it was subsequently unable to persist in the light organ to the usual extent. This persistence phenotype was more severe if the mutant was pregrown under iron‐limiting conditions before inoculation, but could be ameliorated by the presence of excess iron. These results indicate that the ability to respond to iron limitation may be an important requirement in the developing symbiosis. Supplying the glnD gene in trans restored normal efficiency of nitrogen use, iron sequestration and colonization phenotypes to the glnD::mTn5Cm mutant; thus, there appears to be a genetic and/or metabolic linkage between nitrogen sensing, siderophore synthesis and symbiosis competence in V. fischeri that involves the glnD gene.

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“…We used two additional approaches to investigate the role of uridylylation of the GlnK protein with respect to nif regulation. First, we examined the effects of a glnD::Tn10 allele that is known to reduce uridylyltransferase activity greatly (8,9). Second, we examined effects of changing the uridylylated tyrosine in GlnK to another residue.…”

Section: Compare Strain Ncm2087 [Glnk Mutant Strain With Pjes1104]mentioning

confidence: 99%

Physiological Role for the GlnK Protein of Enteric Bacteria: Relief of NifL Inhibition under Nitrogen-Limiting Conditions

Soupène

Ninfa

et al. 1998

J Bacteriol

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In Klebsiella pneumoniae, NifA-dependent transcription of nitrogen fixation (nif) genes is inhibited by a flavoprotein, NifL, in the presence of molecular oxygen and/or combined nitrogen. We recently demonstrated that the general nitrogen regulator NtrC is required to relieve NifL inhibition under nitrogen (N)-limiting conditions. We provide evidence that the sole basis for the NtrC requirement is its role as an activator of transcription for glnK, which encodes a P II -like allosteric effector. Relief of NifL inhibition is a unique physiological function for GlnK in that the structurally related GlnB protein of enteric bacteria-apparently a paralogue of GlnK-cannot substitute. Unexpectedly, although covalent modification of GlnK by uridylylation normally occurs under N-limiting conditions, several lines of evidence indicate that uridylylation is not required for relief of NifL inhibition. When GlnK was synthesized constitutively from non-NtrC-dependent promoters, it was able to relieve NifL inhibition in the absence of uridylyltransferase, the product of the glnD gene, and under N excess conditions. Moreover, an altered form of GlnK, GlnK Y51N , which cannot be uridylylated due to the absence of the requisite tyrosine, was still able to relieve NifL inhibition.

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Regulation of glutamine synthetase formation in Escherichia coli: characterization of mutants lacking the uridylyltransferase

Cited by 55 publications

References 27 publications

Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli

Fine-structure deletion map and complementation analysis of the glnA-glnL-glnG region in Escherichia coli

Novel effects of a transposon insertion in the Vibrio fischeri glnD gene: defects in iron uptake and symbiotic persistence in addition to nitrogen utilization

Physiological Role for the GlnK Protein of Enteric Bacteria: Relief of NifL Inhibition under Nitrogen-Limiting Conditions

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