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Biomedical subjects

E C Cox

Publications and source records attributed to E C Cox.

At least 55 records · Page 3Linked to original sources
PubMed1980

Interaction of an Escherichia coli mutator gene with a deoxyribonucleotide effector.

Strains of Escherichia coli carrying mutD5 display very high mutation rates (about 10(4)-fold above wild-type) when grown in rich medium, but relatively low mutation rates (about 10- to 50-fold above wild-type) in minimal medium. Thymidine, deoxycytidine, and deoxyuridine are all capable of stimulating mutation when added to minimal medium. Studies with mutants blocked in various steps of thymidine metabolism implicate a phosphorylated thymidine effector which mediates the mutagenic action of the added deoxyribonucleotides. In addition, an unidentified compound or compounds other than thymidine present in rich medium (L-broth) can also increase the mutation rate.

Culture Media↗
PubMed1976

Genetic and morphological study of aggregation in the cellular slime mold Polysphondylium violaceum.

A system for genetic analysis in the cellular slime mold P. violaceum has been developed. Two growth-temperature-sensitive mutants were isolated in a haploid strain and used to select rare diploid heterozygotes arising by spontaneous fusion of the haploid cells. A recessive mutation to cycloheximide resistance in one stain enables selection of segregants, which often appear to be aneuploid.-Aggregation-defective (ag-) mutants having a wide range of phenotypes were isolated in both temperature-sensitive strains after nitrosoguanidine treatment, and complementation tests were performed between pairs of these mutants. Of 380 diploids isolated, 32 showed defective aggregation and were considered to contain 2 noncomplenting ag- mutations. Among noncomplementing mutants interallelic complentation is common. Noncomplementing mutants fall into 4 complementation groups, and those within each complementation group are phenotypically similar. Statistical analysis of the results suggests that the number of complementation units involved in aggregation is about 50.

Alleles↗
PubMed1974

Selection for high mutation rates in chemostats.

Competition experiments in chemostats show that mutator populations of Escherichia coli are more fit than wild type. The increased fitness can be explained by the appearance of new mutants better adapted to the chemostat environment. Fitness values vary between chemostats and are strongly correlated (P < 0.001) with fluctuations in population density.

Bacteriological Techniques↗
PubMed1974

Conditional mutator gene in Escherichia coli: isolation, mapping, and effector studies.

A mutator gene, mutD5, whose phenotype is conditional, has been identified in Escherichia coli. By P1 transduction it has been shown to lie at about 5.7 min on the chromosome, being co-transduced with proA and argF. In rich medium, streptomycin- and nalidixic acid-resistant mutation frequencies are 50 to 100 times higher than those in minimal medium. In minimal medium, the mutD5-induced mutation frequencies are still 50 to 100 times above co-isogenic wild-type (mut(+)) levels. Similar results were obtained with all markers tested. Mutant frequencies can be raised by thymidine in the medium at concentrations as low as 0.04 muM, or by the endogenous generation of thymidine from thymine plus a deoxyribosyl donor. Deoxyadenosine, various ribonucleosides, thymine, and 2-deoxyribose do not stimulate mutation. None of these effects are related to growth rate, since growth rate and mutation rate can be decoupled completely.

Chromosome Mapping↗
PubMed1972

Mutator gene studies in Escherichia coli: the mutS gene.

We report here on a study of a mutator gene (mutS) that causes transition mutations in Escherichia coli. We have used the trpA system to show that A:T-->G:C and G:C-->A:T transitions occur. Not all A:T pairs are equally susceptible to mutS action however, since the A:T pair at the trpA223 site reverts at a frequency similar to, if not identical with, the frequency in a mut(+) background. Presumably this is a consequence of neighboring bases, because other A:T pairs are reverted by mutS in the same gene; and an A:T pair in the lac operon is reverted at two widely separated points on the chromosome, and in two orientations relative to the trp sense strand. In addition, we have shown that the mutS1 allele is recessive to wild type, and trans active.

Alleles↗
PubMed1970

Fitness of an Escherichia coli mutator gene.

Competition experiments between Escherichia coli mutT1 and mut(+) populations show that the mutator gene confers selective advantage on the strain that carries it. The observed increase in fitness varies, with an average increase in mutator growth rate of 1.4 percent when mutator and wild-type strains are grown together in chemostats.

DNA Replication↗
PubMed1969

Mutator gene studies in Escherichia coli.

An Escherichia coli mutator gene, mutT, has been shown by P1-mediated crosses to map between the leucine and azide loci. The mutT1 and azi-r alleles cotransduce with a frequency of >92%. In mutT1/mutT(+) merodiploids, the mutT1 phenotype is recessive; in mutT1/F'trp or mutT1/F'lac merodiploids, the mutT1 allele has a trans effect. The gene can mutate lambda and T7 phage but not T1, T3, T4, T5, and S13.

Chromosome Mapping↗
PubMed1969

Anthranilate synthetase, an enzyme specified by the tryptophan operon of Escherichia coli: purification and characterization of component I.

A procedure employed in the purification of anthranilate synthetase component I of Escherichia coli is described. The purified component appears homogeneous by starch gel electrophoresis and by sedimentation analysis. A molecular weight of 60,000 was estimated by gel filtration of Sephadex G-100. This value is consistent with the molecular weight estimated from the sedimentation and diffusion coefficients. Purified anthranilate synthetase component I cannot use glutamine as substrate and thus has no activity in the reaction of chorismate + l-glutamine --> anthranilate; however, it is active when ammonium sulfate is provided as amino donor. Sucrose density gradient analyses showed that ammonium sulfate does not affect the sedimentation velocity of component I. The ultraviolet absorption and fluorescence spectra of the purified component indicated that it contains tryptophan. Peptide pattern and extract complementation evidence suggested that the protein is a single polypeptide chain. Enzyme activity measurements indicated that wild-type E. coli produces equimolar amounts of at least four of the five polypeptides specified by the operon. Purified anthranilate synthetase component I is inhibited by l-tryptophan.

Centrifugation, Density Gradient↗