Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli

Stragier, Patrick; Richaud, F; Borne, Françoise; Patte, Jean‐Claude

doi:10.1016/s0022-2836(83)80020-5

Cited by 86 publications

(53 citation statements)

References 33 publications

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“…The target plasmid (pSRW220 or pSRW226) was transformed into the strain JMlOS(pRU870) with selection for ampicillin and chloramphenicol resistance. Plasmid pRU870 contains the CmR transposon TmZ737Cm (Ubben & Schmitt, 1987) and is compatible with plasmids with pMB1-based replicons such as pSRW220 or pSRW226. Eollowia~g transformation single colonies were left for approximately 2 weeks at room temperature.…”

Section: Methodsmentioning

confidence: 99%

“…In Tn1737Cm the lac2 coding sequence is located at one end (Ubben & Schmitt, 1987). There is no promoter for lucZ within the transposon and so B-galactosidase is only produced if the transposon becomes inserted downstream from a promoter in the correct orientation.…”

Section: Methodsmentioning

confidence: 99%

“…To locate more accurately the position of the gene which had been cloned, transposon mutagenesis of both pSRW220 and pSRW226 was done using Tn1737Cm (Ubben & Schmitt, 1987 of transcription of the mor gene is away from the BamHI site of pSRW226 towards the EcoRI site. Second, the failure to detect transcription of /3-galactosidase with pSRW226.6, even though the insert in this plasmid is in the same orientation as the insert in pSRW226.3, suggested that in the former plasmid insertional inactivation in the region of the rnor promoter has occurred.…”

Section: Cloning Of a Gene From The 89 Minute Region Of The E Coli Cmentioning

confidence: 99%

“…Four proteins showing a high level of homology were identified. These were the iluY, cysB and 1ysR proteins of E. coli (Wek & Hatfield, 1986;Ostrowski et al, 1987;Stragier & Patte, 1983) and the metR protein of Salmonella typhimurium (Plamann & Stauffer, 1987). The percentage homologies that the putative mor gene product exhibits with these four proteins are listed in Table 2.…”

Section: Sequence Of the Mor Genementioning

confidence: 99%

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Identification and Characterization of a Gene that Controls Colony Morphology and Auto-Aggregation in Escherichia Coli K12

Warne

Varley

Boulnois

et al. 1990

Journal of General Microbiology

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Many Escherichia coli K12 strains undergo switching between two forms which differ in a number of surface properties including colony morphology and the ability to auto-aggregate. This paper describes the identification of a gene which appears to play a part in controlling this switching phenomenon. This gene has been designated mor and is located at 89 minutes on the E. coli chromosome map between the argECBHoperon and the trmA gene. By manipulation of this gene it is possible to overcome the switching of surface properties and fix a strain in one form or the other. The mor gene has been cloned and its DNA sequence determined. The putative protein sequence shows a high level of bomology with four regulatory genes, the iluY, cysB and lysR genes from E. coli and the metR gene from Sdmonella typhurium. It has also been shown that the mor gene is autoregulated at the transcriptional level.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Cloning Of a Gene From The 89 Minute Region Of The E Coli Cmentioning

confidence: 99%

Section: Sequence Of the Mor Genementioning

confidence: 99%

See 2 more Smart Citations

Identification and Characterization of a Gene that Controls Colony Morphology and Auto-Aggregation in Escherichia Coli K12

Warne

Varley

Boulnois

et al. 1990

Journal of General Microbiology

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“…No consistent pattern for regulation of the lysine pathway in bacteria has emerged, although repression of enzyme synthesis and enzyme activity has been observed in multiple systems (1)(2)(3). In Escherichia coli, the lysA gene encoding meso-DAP decarboxylase, which carries out the final step in lysine biosynthesis, is regulated at the level of transcription initiation by the LysR transcriptional activator (4). Repression of Bacillus subtilis lysA by lysine was reported, but the mechanism is unknown (5).…”

mentioning

confidence: 99%

The L box regulon: Lysine sensing by leader RNAs of bacterial lysine biosynthesis genes

Grundy

Lehman

Henkin

2003

Proc. Natl. Acad. Sci. U.S.A.

173

149

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Expression of amino acid biosynthesis genes in bacteria is often repressed when abundant supplies of the cognate amino acid are available. Repression of the Bacillus subtilis lysC gene by lysine was previously shown to occur at the level of premature termination of transcription. In this study we show that lysine directly promotes transcription termination during in vitro transcription with B. subtilis RNA polymerase and causes a structural shift in the lysC leader RNA. We find that B. subtilis lysC is a member of a large family of bacterial lysine biosynthesis genes that contain similar leader RNA elements. By analogy with related regulatory systems, we designate this leader RNA pattern the ''L box.'' Genes in the L box family from Gram-negative bacteria appear to be regulated at the level of translation initiation rather than transcription termination. Mutations of B. subtilis lysC that disrupt conserved leader features result in loss of lysine repression in vivo and loss of lysine-dependent transcription termination in vitro. The identification of the L box pattern also provides an explanation for previously described mutations in both B. subtilis and Escherichia coli lysC that result in lysC overexpression and resistance to the lysine analog aminoethylcysteine. The L box regulatory system represents an example of gene regulation using an RNA element that directly senses the intracellular concentration of a small molecule.

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Metabolic pathways and fermentative production of L‐aspartate family amino acids

Park

Lee

2010

Biotechnology Journal

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The L-aspartate family amino acids (AFAAs), L-threonine, L-lysine, L-methionine and L-isoleucine have recently been of much interest due to their wide spectrum of applications including food additives, components of cosmetics and therapeutic agents, and animal feed additives. Among them, L-threonine, L-lysine and L-methionine are three major amino acids produced currently throughout the world. Recent advances in systems metabolic engineering, which combine various high-throughput omics technologies and computational analysis, are now facilitating development of microbial strains efficiently producing AFAAs. Thus, a thorough understanding of the metabolic and regulatory mechanisms of the biosynthesis of these amino acids is urgently needed for designing system-wide metabolic engineering strategies. Here we review the details of AFAA biosynthetic pathways, regulations involved, and export and transport systems, and provide general strategies for successful metabolic engineering along with relevant examples. Finally, perspectives of systems metabolic engineering for developing AFAA overproducers are suggested with selected exemplary studies.

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Regulation of diaminopimelate decarboxylase synthesis in Escherichia coli

Cited by 86 publications

References 33 publications

Identification and Characterization of a Gene that Controls Colony Morphology and Auto-Aggregation in Escherichia Coli K12

Identification and Characterization of a Gene that Controls Colony Morphology and Auto-Aggregation in Escherichia Coli K12

The L box regulon: Lysine sensing by leader RNAs of bacterial lysine biosynthesis genes

Metabolic pathways and fermentative production of L‐aspartate family amino acids

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