Biomedical subjects

C M Hardy

Publications and source records attributed to C M Hardy.

23 records · Page 2Linked to original sources

PubMed1985

Pi exchange mediated by the GlpT-dependent sn-glycerol-3-phosphate transport system in Escherichia coli.

The GlpT system for sn-glycerol-3-phosphate transport in Escherichia coli is shown to catalyze a rapid efflux of Pi from the internal phosphate pools in response to externally added Pi or glycerol-3-phosphate. A glpR mutation, which results in constitutive expression of the GlpT system, is responsible for this rapid Pi efflux and the arsenate sensitivity of several laboratory strains, including the popular strain C600. Glucose and other phosphotransferase system sugars inhibit Pi efflux by repressing glpT expression.

Arsenates↗

PubMed1984

Characterization of Barmah forest virus: an alphavirus with some unusual properties.

Barmah Forest virus has been characterized in a number of ways including electron microscopy of infected cells; physical studies of the virion, its RNA, and associated proteins; N-terminal sequence analysis of the two envelope glycoproteins; studies of macromolecular species present in infected cells; and serological cross-reactions with alphaviruses and bunyaviruses. From these results Barmah Forest virus is clearly an alphavirus since the structure of the virion, the mode of replication, and the macromolecular species present in infected cells are typical of alphaviruses. The N-terminal regions of the two glycoproteins E1 and E2 show extensive sequence homology (approximately 50%) with those of other alphaviruses. Barmah Forest virus cross-reacts in hemagglutination inhibition tests, although not in complement fixation tests or infectivity neutralization tests, with other alphaviruses. In some of its properties Barmah Forest virus is unusual, however. It cross-reacts in complement fixation and hemagglutination inhibition tests with Umbre virus, a bunyavirus, which originally led it to be classified as a bunyavirus; the glycosylation pattern of E2 of Barmah Forest virus appears to differ from that of other alphaviruses; and the sedimentation coefficient of the virion appears to be slightly less than that of other alphaviruses.

Aedes↗

PubMed1984

Rapid turnover of mannitol-1-phosphate in Escherichia coli.

The phosphate moiety of D-mannitol-1-phosphate in Escherichia coli is subject to rapid turnover and is in close equilibrium with Pi and the phosphorus of fructose-1,6-bisphosphate. These three compounds account for the bulk of 32P label found in cells after several minutes of uptake of 32Pi and mannitol-1-phosphate represents some 30% of this label. Mannitol-1-phosphate occurs in E. coli grown on a variety of carbon sources, in the absence of D-mannitol, and is synthesized de novo even in mutants lacking mannitol-1-phosphate dehydrogenase. The mannitol moiety of mannitol-1-phosphate was not affected during the total chase of the P moiety, which exchanged with a half-life of about 30 s. These findings suggest that the rapid equilibration of the phosphorus is a function of an enzyme, possibly a component of the phosphotransferase system, capable of forming a complex that allows the exchange of the phosphate without the equilibration of the mannitol moiety with free mannitol.

Escherichia coli↗

PubMed1984

Conversion of D-mannitol to D-ribose: a newly discovered pathway in Escherichia coli.

A mutant (mtlD) strain of Escherichia coli unable to oxidize mannitol-1-phosphate to fructose-6-phosphate was used to study the fate of mannitol-1-phosphate. D-[1-14C]mannitol entered the cells via the phosphotransferase system and was phosphorylated equally at carbon 1 or 6. The label disappeared gradually from the mannitol-1-phosphate pool, and some 60% of the 14C was recovered in nucleic acids. Ribose was isolated from the purified RNA. The 14C label distribution in the isolated ribose precluded a simple hexose-to-pentose conversion by elimination of one terminal carbon from mannitol-1-phosphate. The 14C from mannitol-1-phosphate that did not enter macromolecules was found in CO2 and in some organic, non-phosphorylated compounds that were not identified. We suggest that the de novo synthesis of mannitol-1-phosphate in E. coli may be a reaction specifically dedicated to the biosynthesis of ribose.

Carbon Dioxide↗

PubMedDate not supplied

Nucleotide sequence of the cytochrome oxidase subunit 2 and val-tRNA genes and surrounding sequences from Kluyveromyces lactis K8 mitochondrial DNA.

The nucleotide sequence of the cytochrome oxidase subunit 2 (cox2) and val-tRNA genes and surrounding regions from Kluyveromyces lactis mitochondrial DNA is reported. Analysis of the coding region shows that the codons CUN (Thr), CGN (Arg) and AUA (Met) are absent in this gene. A single sequence, ATATAAGTAA, identical to the baker's yeast mtRNA polymerase recognition site, was detected upstream of val-tRNA. This sequence is absent from regions between val-tRNA-cox2 and cox2-cox1. In addition a sequence AATAATATTCTT, identical to the mRNA processing site in other yeast mitochondrial genomes is present 32-43 bp downstream to the TAA stop codon for the cox2 gene. Another short conserved sequence of 5 bp, TCTAA, is present upstream of the coding regions of cox2 genes in several yeasts, including K. lactis, but is not present upstream of other genes. Comparison of cox2 sequences from other organisms indicates that the mitochondrial DNA of K. lactis is closely related to that of Saccharomyces cerevisiae.

Amino Acid Sequence↗