Cloning of the Glutamyl-tRNA Synthetase (
            <i>gltX</i>
            ) Gene from
            <i>Pseudomonas aeruginosa</i>

Franklund, C V; Goldberg, Joanna B.

doi:10.1128/jb.181.11.3582-3586.1999

Cited by 4 publications

(2 citation statements)

References 22 publications

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“…CC9605. Localization of gltX adjacent to tRNA genes seems to be frequent in prokaryotes (Brun et al, 1990;Franklund and Goldberg, 1999). In contrast, none of the cyanobacterial genomes checked contains an insertion element between gltX and the gene upstream of it.…”

Section: Resultsmentioning

confidence: 99%

Regulated expression of glutamyl‐tRNA synthetase is directed by a mobile genetic element in the cyanobacterium Tolypothrix sp. PCC 7601

Luque

Andújar

Jia

et al. 2006

Molecular Microbiology

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SummaryThe genome of Tolypothrix sp. PCC 7601 carries two copies of a novel insertion sequence, IS Tosp 1. One of the two copies is located upstream of the gene encoding glutamyl-tRNA synthetase, an enzyme playing a key role in protein and pigment synthesis. The tnpA gene of the IS element and gltX were co-transcribed and their expression was transiently upregulated upon retrieval of the ammonium source irrespective of whether nitrate or no nitrogen source were available. The second copy is also transcribed and shows a similar regulatory pattern. Structural elements of the promoter ( -10 and -35 sequences) directing the expression of the tnpA-gltX operon have been localized within the IS. Regulatory sequences involving the NtcA transcription factor in the control of tnpA-gltX expression were found both within and in sequences upstream of the insertion element. The expression of gltX in a closely related cyanobacterium, Nostoc sp. PCC 7120, which lacks the insertion upstream of gltX , decreased upon ammonium retrieval, a regulatory pattern that markedly differs from that observed in Tolypothrix sp. PCC 7601. IS Tosp 1 constitutes a good example of how cells can make use of a transposable element to evolve an original regulatory mechanism.

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Section: Resultsmentioning

confidence: 99%

Regulated expression of glutamyl‐tRNA synthetase is directed by a mobile genetic element in the cyanobacterium Tolypothrix sp. PCC 7601

Luque

Andújar

Jia

et al. 2006

Molecular Microbiology

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“…Conserved Domain Search showed that the conserved HIGH and KMSKS motifs also existed in the catalytic domain of C. glutamicum GluRS (Additional file 1 : Figure S1). GluRS from C. glutamicum probably belonged to the Class I synthetase that aminoacylates the 3′ hydroxyl group of the cognate tRNA [ 16 ]. Glutamyl-tRNA reductase (HemA) was predicted to be encoded by hemA .…”

Section: Resultsmentioning

confidence: 99%

Engineering Corynebacterium glutamicum to produce 5-aminolevulinic acid from glucose

Jin

Liu

et al. 2015

Microb Cell Fact

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BackgroundCorynebacterium glutamicum is generally regarded as a safe microorganism and is used to produce many biochemicals, including l-glutamate. 5-Aminolevulinic acid (ALA) is an l-glutamate derived non-protein amino acid, and is widely applied in fields such as medicine and agriculture.ResultsThe products of the gltX, hemA, and hemL genes participate in the synthesis of ALA from l-glutamate. Their annotated C. glutamicum homologs were shown to be functional using heterologous complementation and overexpression techniques. Coexpression of hemA and hemL in native host led to the accumulation of ALA, suggesting the potential of C. glutamicum to produce ALA for research and commercial purposes. To improve ALA production, we constructed recombinant C. glutamicum strains expressing hemA and hemL derived from different organisms. Transcriptome analysis indicated that the dissolved oxygen level and Fe2+ concentration had major effects on ALA synthesis. The downstream pathway of heme biosynthesis was inhibited using small molecules or introducing genetic modifications. Small-scale flask cultures of engineered C. glutamicum produced 1.79 g/L of ALA.ConclusionFunctional characterization of the key enzymes indicated complex regulation of the heme biosynthetic pathway in C. glutamicum. Systematic analysis and molecular genetic engineering of C. glutamicum may facilitate its development as a system for large-scale synthesis of ALA.Electronic supplementary materialThe online version of this article (doi:10.1186/s12934-015-0364-8) contains supplementary material, which is available to authorized users.

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Comparative genomics and informational content analysis uncovered internal regions of the core genes rpoD, pepN and gltX for an MLSA with genome-level resolving power within the genus Pseudomonas

Garavaglia

Muzlera²,

Valverde³

2023

Molecular Phylogenetics and Evolution

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Cloning of the Glutamyl-tRNA Synthetase ( gltX ) Gene from Pseudomonas aeruginosa

Cited by 4 publications

References 22 publications

Regulated expression of glutamyl‐tRNA synthetase is directed by a mobile genetic element in the cyanobacterium Tolypothrix sp. PCC 7601

Regulated expression of glutamyl‐tRNA synthetase is directed by a mobile genetic element in the cyanobacterium Tolypothrix sp. PCC 7601

Engineering Corynebacterium glutamicum to produce 5-aminolevulinic acid from glucose

Comparative genomics and informational content analysis uncovered internal regions of the core genes rpoD, pepN and gltX for an MLSA with genome-level resolving power within the genus Pseudomonas

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