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P Gay

Publications and source records attributed to P Gay.

At least 37 records · Page 2Linked to original sources
PubMed1986

[Locus ref(2)P of Drosophila melanogaster. I. Cytogenetic localization of ref(2)P].

The ref(2)P gene is a Drosophila gene which acts on Sigma virus multiplication. From recombination experiments the ref(2)P gene was located between hk and pr. This location was confirmed by the study of eight chromosomic aberrations, without ref(2)P gene activity, obtained following X irradiation. From the cytological study of three of these chromosomes and from the study of the ref(2)P gene activity of chromosomic aberrations obtained by other workers in the same region of the second chromosome, the ref(2)P gene was cytologically located in 37E3-37F3.

Animals↗
PubMed1986

Grand illusions.

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Historiography↗
PubMed1985

The DNA sequence of the gene for the secreted Bacillus subtilis enzyme levansucrase and its genetic control sites.

We present the sequence of a 2 kb fragment of the Bacillus subtilis Marburg genome containing sacB, the structural gene of levansucrase, a secreted enzyme inducible by sucrose. The peptide sequence deduced for the secreted enzyme is very similar to that directly determined by Delfour (1981) for levansucrase of the non-Marburg strain BS5. The peptide sequence is preceded by a 29 amino acid signal peptide. Codon usage in sacB is rather different from that in the sequenced genes of other secreted enzymes in B. subtilis, especially alpha-amylase. Genetic evidence has shown that the sacB promotor is rather far from the beginning of sacB (200 bp or more). The 200 bp region preceding sacB shows some of the features of an attenuator. A preliminary discussion of the putative workings and roles of this attenuator-like structure is proposed. sacRc mutations, which allow constitutive expression of levansucrase, have been located within the 450 bp upstream of sacB. It is shown that sacRc and sacR+ alleles control in cis the expression of the adjacent sacB gene.

Amino Acid Sequence↗
PubMed1985

Positive selection procedure for entrapment of insertion sequence elements in gram-negative bacteria.

We constructed the broad-host-range plasmid pUCD800 containing the sacB gene of Bacillus subtilis for use in the positive selection and isolation of insertion sequence (IS) elements in gram-negative bacteria. Cells containing pUCD800 do not grow on medium containing 5% sucrose unless the sacB gene is inactivated. By using pUCD800, we isolated a 1.4-kilobase putative IS element from Agrobacterium tumefaciens NT1RE by selection for growth on sucrose medium. This putative IS element appears to be unique to Agrobacterium strains.

Bacillus subtilis↗
PubMed1983

[Genetic analysis of sacB, the structural gene of a secreted enzyme, levansucrase of Bacillus subtilis Marburg].

The structural gene sacB encoding B. subtilis levansucrase, a secreted enzyme, expresses in E. coli. E. coli hosts of the sacB gene are poisoned by sucrose. This property allowed a powerful selection of mutants affected in the cloned gene. The plasmidic mutations were readily introduced in the B. subtilis chromosome. Using a collection of plasmids bearing various deletions extending in sacB we developed a technique of deletion mapping based on plasmid integration in the chromosome of B. subtilis. A generalization of this technique is discussed.

Bacillus subtilis↗
PubMed1983

Chromosomal localization of gut, fruC, and pfk mutations affecting genes involved in Bacillus subtilis D-glucitol catabolism.

Mutations affecting the genes involved in B. subtilis D-glucitol catabolism were mapped either by PBS1-mediated transduction or DNA-mediated transformation. It was shown that the genes gutA and gutB coding for the D-glucitol permease and the D-glucitol dehydrogenase, respectively, and regulatory locus gutR are clustered in a gut operon localized between purB and dal close to the pha marker. A mutation affecting fructokinase activity (fruC) was mapped near the gut markers. The fruC gene does not belong to the operon. A mutation affecting phosphofructokinase activity (pfk) was mapped between the leuA and aroG markers.

Bacillus subtilis↗
PubMed1983

Cloning structural gene sacB, which codes for exoenzyme levansucrase of Bacillus subtilis: expression of the gene in Escherichia coli.

A clone bearing the structural gene sacB, coding for the exoenzyme levansucrase, was isolated from a library of Bacillus subtilis DNA that was cloned in phage lambda charon 4A on the basis of the transforming activity of the chimeric DNA. This lambda clone also was found to contain the sacR and smo loci. Subcloning the sacB-sacR region in plasmid pBR325 resulted in a clone which directed levansucrase synthesis in Escherichia coli. The nucleotide sequence coding for the secreted protein was localized on the physical map of the cloned DNA.

Bacillus subtilis↗
PubMed1983

Get it in writing.

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Inservice Training↗
PubMed1979

Characterisation of post exercise pressure response curves in the pedal arteries of patients with peripheral vascular disease.

The response of the systolic pressure in the pedal arteries to the stress of exercise is one of several ways of assessing the severity of peripheral vascular disease. We have examined 2607 such pressure response curves in an attempt to produce a simple method of response classification. Regression analysis of the curves has shown that errors are least when the regression used is the same order as the number of data points. We conclude that post exercise response curves can be adequately classified from three data points, one obtained within two minutes of the cessation of exercise, a second obtained between 4 and 6 minutes from the end of exercise and a third taken 10 minutes after exercise. The use of a response curve indexed to systemic systolic pressure was not found to produce a better correlation between full and three point curves, though the absolute classification differed slightly from that obtained from the non-indexed curve. Neither classification system proved significantly superior in relating to the degree of arterial disease.

Arteries↗
PubMed1979

Filtration of debris from banked blood.

Commercially available filters will effectively remove microaggregates from stored blood. The combined results of screen filtration pressure (SFP), debris weight, and particle size analysis offer a reproducible means of evaluating different filters. The effectiveness of three blood filters (Fenwal, Bentley, and Pall) is evaluated using SFP, debris weight measurement, particle size analysis, and determinations of filter capacity. Of the filters studied the Fenwal filter provides the most efficient means of removing debris while maintaining adquate flow rates for relatively large volumes of blood. The filter appears comparable to the Swank filter in overall effectiveness and flow characteristics.

Blood↗
PubMed1979

Kinetic study of a phosphoryl exchange reaction between fructose and fructose 1-phosphate catalyzed by the membrane-bound enzyme II of the phosphoenolpyruvate-fructose 1-phosphotransferase system of Bacillus subtilis.

A phosphoryl exchange reaction between fructose 1-phosphate and fructose was found to be catalyzed by a membrane preparation isolated from Bacillus subtilis. The regulation of the biosynthesis of the activity in the wild type as well as in the regulation mutants fruB closely correlates with that of the membrane-bound enzyme II of the phosphoenolpyruvate fructose 1-phosphotransferase system which is known to mediate the transmembrane vectorial phosphorylation of fructose. The computed analysis of the kinetic data shows that the mechanism of the enzyme II is ping-pong, i.e. that a phosphoryl-enzyme intermediate occurs in the reaction. The apparent dissociation constants of the enzyme II/fructose 1-phosphate complex and of the phosphoryl enzyme II/fructose complex are estimated. The value of the standard free energy of the hydrolysis of the bond between the phosphoryl moiety and the enzyme suggests a covalent bonding. This intermediate is assumed to occur in the physiological functioning of the enzyme which utilizes the phosphocarrier protein HPr as phosphoryl donor. The exchange reaction is competitively inhibited by high fructose concentrations: this indicates that the same site of the enzyme binds fructose and fructose 1-phosphate, this site being accessible to fructose on the external side of the membrane when the enzyme is phosphorylated.

Bacillus subtilis↗
PubMed1978

Biochemical and genetic study of D-glucitol transport and catabolism in Bacillus subtilis.

The catabolic pathway of D-glucitol (sorbitol) in Bacillus subtilis Marburg 168M is characterized. It includes (i) a transport step catalyzed by a D-glucitol permease which is affected by the gutA mutations, (ii) an oxidation step of the intracellular D-glucitol catalyzed by a D-glucitol dehydrogenase, generating intracellular fructose, affected by gutB mutations, and (iii) phosphorylation of the intracellular fructose either at the C1 site or at the C6 site as described previously (A. Delobbe et al., Eur. J. Biochem., 66:485-491, 1976; A. Delobbe et al., EUR. J. Biochem. 51:503-510, 1975). Additional data are given concerning the phosphorylation of fructose by a fructokinase (fructose ATP 6-phosphotransferase), which is affected by the fruC mutation. The isolation of regulatory mutants affected in gutR that synthesize constitutively both the permease and the dehydrogenase indicates the existence of a D-glucitol operon in B. subtilis. Unlike the wild-type strain, these mutants are able to utilize D-xylitol as sole carbon source.

Bacillus subtilis↗