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I Saint-Girons

Publications and source records attributed to I Saint-Girons.

28 records · Page 2Linked to original sources
PubMed1982

Attenuation in the threonine operon: effects of amino acids present in the presumed leader peptide in addition to threonine and isoleucine.

We have studied in vivo the contribution of amino acids corresponding to codons of the leader sequence other than the so-called "regulatory codons" (for threonine and isoleucine) in the expression of the threonine operon. In the presence of threonine and isoleucine, addition of each amino acid encoded in the proximal part of the leader sequence resulted in a significant decrease of the expression of the operon, over and above that decrease observed in the sole presence of threonine and isoleucine. These effects were cumulative. No such effect was found with the amino acids encoded by the distal part of the leader sequence. These findings are discussed in the light of the current model of attenuation.

Amino Acid Sequence↗
PubMed1981

Integration specificity of an artificial kanamycin transposon constructed by the in vitro insertion of an internal Tn5 fragment into IS2.

IS2 has been marked genetically by the in vitro insertion into its HindIII site of a 3.3 Kb HindIII fragment of Tn5 conferring resistance to kanamycin. The transposition of the IS2::Km, thus obtained, to lambda has been found and insertion sites were characterised. Each of ten independent IS2::Km insertions were found at the same site at 61.2% of the lambda map, always in the same orientation (orientation II relative to the xis gene). The integration sites of IS2::Km in five of the kanamycin-transducing phages were determined by DNA sequence analysis, and were found to be identical at the nucleotide level. Further transposition of IS2::Km from lambda to the bacterial chromosome was demonstrated.

Bacteriophage lambda↗
PubMed1980

Nucleotide sequence of the thrA gene of Escherichia coli.

The thrA gene of Escherichia coli codes for a single polypeptide chain having two enzymatic activities required for the biosynthesis of threonine, aspartokinase I and homoserine dehydrogenase I. This gene was cloned in a bacterial plasmid and its complete nucleotide sequence was established. It contains 2460 base pairs that encode for a polypeptide chain of 820 amino acids. The previously determined partial amino acid sequence of this protein is in good agreement with that predicted from the nucleotide sequence. The gene contains an internal sequence that resembles the structure of bacterial ribosome-binding sites, with an AUG preceded by four triplets, each of which can be converted to a nonsense codon by a single mutation. This suggests that the single polypeptide chain was formed by the fusion of two genes and that initiation of translation may occur inside the gene to give a protein fragment having only the homoserine dehydrogenase activity.

Aspartokinase Homoserine Dehydrogenase↗
PubMed1978

New regulatory mutations affecting the expression of the threonine operon in Escherichia coli K-12.

The promoter of the threonine operon was joined to the structural genes of the lac operon in Escherichia coli K 12. The synthesis of beta-galactosidase was thus repressed by threonine plus isoleucine in the fusion strains. To isolate mutations which affect the expression of the threonine operon, alterations in the level of expression of the lacZ gene were selected. A new type of regulatory mutation was discovered.

Escherichia coli↗
PubMed1978

Fine structure analysis of the threonine operon in Escherichia coli K-12.

A fine structure analysis of the threonine operon in Escherichia coli K-12 was performed by deletion mapping. Lambda transducing bacteriophages carrying various parts of the threonine operon were isolated from strains in which the lacZ gene was fused to a thr gene. We tested for recombination between deletions of the threonine promotor extending into the threonine operon, carried by the phage, and bacterial thr auxotrophs. The relative order of thrO (operator) mutations was established. We propose that an operator region is located between a promoter region and the structural genes. Mutations leading to the desensitization of the aspartokinase I-homoserine dehydrogenase I towards threonine were localized in two different regions of the thrA gene.

Aspartokinase Homoserine Dehydrogenase↗
PubMed1977

Threonyl-transfer ribonucleic acid synthetase and the regulation of the threonine operon in Escherichia coli.

Two threonine-requiring mutants with derepressed expression of the threonine operon were isolated from an Escherichia coli K-12 strain containing two copies of the thr operon. One of them carries a leaky mutation in ilvA (the structural gene for threonine deaminase), which creates an isoleucine limitation and therefore derepression of the thr operon. In the second mutant, the enzymes of the thr operon were not repressed by threonine plus isoleucine; the threonyl-transfer ribonucleic acid(tRNA) synthetase from this mutant shows an apparent Km for threonine 200-fold higher than that of the parental strain. The gene, called thrS, coding for threonyl-tRNA synthetase was located around 30 min on the E. coli map. The regulatory properties of this mutant imply the involvement of charged threonyl-tRNA or threonyl-tRNA synthetase in the regulation of the thr operon.

Amino Acyl-tRNA Synthetases↗
PubMed1975

Operator-constitutive mutants in the threonine operon of Escherichia coli K-12.

Three Escherichia coli K-12 mutant strains resistant to DL-alpha-amino-beta-hydroxyvaleric acid were isolated in which the expression of the thr operon is constitutive. The localization and dominance properties of the mutations involved, called thrO, are those of operator mutations. The gene sequence is OABC as suggested by earlier studies.

Aspartate Kinase↗
PubMed1974

Threonine locus of Escherichia coli K-12: genetic structure and evidence for an operon.

Three genes, thrA, thrB, and thrC, were previously defined and localized in the threonine locus of Escherichia coli K-12. thrA, thrB, and thrC specify the enzymes aspartokinase I-homoserine dehydrogenase I, homoserine kinase, and threonine synthetase, respectively. A complementation analysis of the threonine cluster using derivatives of a lambda phage carrying the threonine genes (lambdadthr(c)) demonstrates that: (i) thrB and thrC each consist of a single cistron; and (ii) thrA is composed of two cistrons, thrA(1) and thrA(2), although it specifies a single polypeptide chain. thrA(1) and thrA(2) correspond to aspartokinase I and homoserine dehydrogenase I, respectively. Their relative order is established. The demonstration of polar effects of mutations (nonsense or induced by phage Mu) in thrA and thrB is taken as evidence for the existence of a thrA thrB thrC operon, transcribed in this order.

Alcohol Oxidoreductases↗
PubMedDate not supplied

First isolation and characterisation of Borrelia garinii, agent of Lyme borreliosis, from Irish ticks.

Nymphal Ixodes ricinus, the tick vector of Lyme borreliosis, were collected from the edges of paths in Muckross Demesne, Killarney National Park, Co. Kerry, Ireland. Examination of some of these nymphs by indirect immunofluorescence showed an infection prevalence of 12% with Borrelia burgdorferi sensu lato, the spirochaete agent of Lyme borreliosis. Gerbils (Meriones unguiculatus) were infected by infesting them with other nymphs from the same batch. Subsequently uninfected laboratory larvae were applied to the gerbils and the contents of the resulting infected engorged ticks were then placed in media and the spirochaetes cultured. The spirochaetes were identified as B. burgdorferi sensu lato by indirect immunofluorescence using monoclonal antibodies and they were further characterised by polymerase chain reaction and pulsed-field gel electrophoresis. Both of these latter techniques showed that spirochaetes in all samples belonged to the genomic species, Borrelia garinii.

Animals↗