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Biomedical subjects

A Ullmann

Publications and source records attributed to A Ullmann.

At least 73 records · Page 4Linked to original sources
PubMed1988

Bordetella pertussis adenylate cyclase: the gene and the protein.

Using the adenylate cyclase-calmodulin interaction as a tool, the B. pertussis cya gene was cloned in a cya defective E. coli strain harbouring a plasmid which expressed high levels of calmodulin. The determination of the nucleotide sequence of the gene showed that adenylate cyclase is synthesized as a large precursor of 1706 amino acids. The calmodulin-stimulated catalytic activity resides in the amino-terminal 400 amino acids whereas the 1300 amino acid carboxy-terminal part of the precursor is endowed with haemolytic activity. The catalytically active 43 kDa form of adenylate cyclase is organized in two domains: the N-terminal domain of 25 kDa harbors the catalytic site, and the 18 kDa C-terminal domain carries the main calmodulin-binding site. Immunological relatedness established between B. pertussis, B. anthracis and rat brain adenylate cyclases suggests a common evolutionary origin of a central domain of these calmodulin-stimulated enzymes. The secretion of the adenylate cyclase-haemolysin bifunctional protein (cyclolysin) requires the expression of three additional genes, contiguous to the cya gene. These four genes appear to form a single operon. The mechanism of secretion of the bifunctional protein should be similar to that described for E. coli alpha-haemolysin.

Adenylate Cyclase Toxin↗
PubMed1986

Properties of cyclic AMP-independent catabolite gene activator proteins of Escherichia coli.

The protein products of two crp alleles encoding mutationally altered catabolite gene activator proteins CAP and CAPc, which are functionally active in vivo in the absence of cAMP, were purified by an immunoaffinity purification procedure. These proteins bind cAMP with the same affinity as does the wild-type catabolite gene activator protein. From their susceptibility to the proteolytic enzyme subtilisin, we conclude that the two mutationally altered proteins adopt structural features adequate for biological activity and similar to the conformation that cAMP elicits or stabilizes in wild-type catabolite gene activator protein. We note, however, that their conformation is not unique and can be modulated by cAMP. The two altered proteins, CAP and CAPc, bind to the lactose promoter, giving rise to specific DNA-protein complexes in the absence of cAMP and promote initiation of specific lac messenger RNA synthesis.

Alleles↗
PubMed1985

Catabolite repression 1985.

The present status of catabolite repression is summarized with respect to the involvement of cyclic AMP and other mediators. A model is presented which may account for the relationship between positive control of gene expression exerted by cAMP and its receptor, CAP, and negative control of catabolite repression mediated by specific metabolites.

Bacteria↗
PubMed1985

A gerontology internship program for medical students.

Although the aged are the country's major users of medical care and social services, traditional medical school curricula devote little time to the aged and their social needs. This article reports on a community-based gerontology internship established for pre-clinical medical students to sensitize them to the needs of the elderly in the community. Students were assigned to community agencies servicing the elderly; working with elderly clients, they learned about needs and services. Students, agency staff and program faculty found the internship a meaningful, consciousness-raising experience, and an excellent vehicle for preparing future physicians to interact with and care for their aged patients.

Aged↗
PubMed1984

Identification of the Escherichia coli cya gene product as authentic adenylate cyclase.

The Escherichia coli cya gene has been fused in the same register with the lacZ gene. The corresponding hybrid cya-lacZ gene is expressed as a bifunctional protein that exhibits both adenylate cyclase and beta-galactosidase activities, thus proving that cya is the structural gene for adenylate cyclase. The hybrid protein was purified to homogeneity and has been used to raise antibodies that recognize wild-type adenylate cyclase. Finally, the protein has been submitted to amino acid sequence analysis. It has been found that the first ten amino acids fit the predicted sequence obtained from DNA sequence analysis, thus substantiating the prediction that the cya translation initiation codon is UUG .

Adenylyl Cyclases↗
PubMed1984

Transcriptional control of polarity in Escherichia coli by cAMP.

In Escherichia coli, 3'5'-adenosine cyclic monophosphate (cAMP) and its receptor protein (CAP) are known to be involved in the control of transcription initiation of catabolic operons. In previous papers we have shown that the cAMP-CAP complex is also involved as a modulator of polarity in polycistronic transcription units. Furthermore we showed that there exists a functional relationship between this complex and the transcription termination protein, Rho. In this work, we measured mRNA synthesis corresponding to the promoter proximal and distal parts of the lac and gal operons by DNA-RNA hybridization. We show that in these operons the main polarity effect is essentially transcriptional and the cAMP-CAP complex decreases polarity by interfering with premature transcription termination.

Base Sequence↗
PubMed1984

Regulation of cyclic AMP synthesis in Escherichia coli K-12: effects of the rpoD800 sigma mutation, glucose, and chloramphenicol.

An immediate 12-fold inhibition in the rate of beta-galactosidase synthesis occurs in Escherichia coli cells containing the mutant sigma allele rpoD800 after a shift to 42 degrees C. In the present study we characterize the nature of the inhibition. The severe inhibition of beta-galactosidase synthesis was partly relieved by cyclic AMP (cAMP). We inferred that the inhibition might be mediated by a decreased intracellular concentration of cAMP. Consistent with this inference, the rate of cAMP accumulation in mutant cells after a temperature upshift was depressed relative to that in wild-type cells. Glucose and chloramphenicol, two agents known to inhibit differentially beta-galactosidase mRNA synthesis, caused a similar inhibition in the rate of cAMP accumulation. Thus, three diverse stimuli, glucose, chloramphenicol, and a temperature-sensitive sigma mutation, appear to affect beta-galactosidase synthesis by regulating the synthesis of cAMP.

Chloramphenicol↗
PubMed1984

A social work perspective on ethical practice in end-stage renal disease.

Social workers increasingly are defining problems that they encounter in practice in health settings as ethical dilemmas. A distinction is made between those practice questions that can best be answered by an appeal to theoretical or empirical knowledge and expertise (clinical questions) and those which invoke values and ethical imperatives (ethical questions). End-stage renal disease poses in high relief the practice dilemmas that are encountered by social workers and offers an opportunity to explore and clarify issues in resolving them. Using an exchange framework as a basis for analysis, common ethical problems of end-stage renal services are discussed.

Adult↗
PubMed1983

Two functional domains in adenylate cyclase of Escherichia coli.

To study the regulation of Escherichia coli adenylate cyclase, plasmids that carry part of the cya gene, as well as plasmids containing hybrid genes having part of cya fused to part of lacZ, were constructed. This allowed us to propose that the enzyme is made of at least two well-defined domains. The NH2 terminus carries the ATP leads to cAMP catalytic activity, whereas the COOH-terminal end corresponds to a regulatory polypeptide domain.

Adenylyl Cyclases↗
PubMed1982

Multiple regulation of the activity of adenylate cyclase in Escherichia coli.

We have studied the correlation between the activities of adenylate cyclase (ATP pyrophosphatelyase-(cyclizing); EC 4.6.1.1) and in vivo rates of synthesis and intracellular concentrations of adenosine 3',5' cyclic monophosphate (cAMP) under various growth conditions in wild-type Escherichia coli and in mutants lacking or overproducing the cAMP receptor protein (CAP). We showed that when wild-type bacteria are grown in the presence of a variety of carbon sources the intracellular concentrations of cAMP are inversely related to the adenylate cyclase activities determined in permeabilized cells, suggesting that the carbon source-dependent modulation of cAMP levels is not directly related to the regulation of adenylate cyclase activity. In mutants lacking functional CAP (crp) the in vivo rates of cAMP synthesis are several hundred-fold higher than in the wild-type parent without a parallel increase of adenylate cyclase activities. In a strain carrying multiple copies of the crp gene and overproducing CAP the activity of adenylate cyclase is severely inhibited, although the in vivo rate of cAMP synthesis is similar to the parental strain. We interpret these results as indicating that CAP controls mainly the activity rather than the synthesis of adenylate cyclase.

Adenylyl Cyclases↗
PubMed1981

Transcription-translation coupling and polarity: a possible role of cyclic AMP.

Using specific mutants exhibiting altered translational rates we found that when the rate of protein synthesis is reduced the polarity of the lactose and galactose operons is increased. This polarity is in part relieved by cyclic AMP. On the basis of in vitro hybridization experiments were propose that the cyclic AMP-CAP complex and the ribosomes display similar functions, namely destabilization of the RNA-DNA hybrid formed during transcription.

Bacteria↗
PubMed1981

Regulation of galactose operon expression: glucose effects and role of cyclic adenosine 3',5'-monophosphate.

We studied the following two aspects of the glucose effect on galactose operon expression in Escherichia coli K-12: catabolite repression and inducer exclusion. Using both inducible and constitutive strains and measuring the rate of promoter-proximal enzyme synthesis, we found that the galactose operon did not seem to exhibit catabolite repression. The only glucose effect on galactose operon expression which we observed was inducer exclusion, as shown by the existence of diauxic growth in the presence of glucose and galactose. This diauxie was not relieved by cyclic adenosine 3',5'-monophosphate. Cyclic adenosine 3',5'-monophosphate did not seem to be an antagonist of any glucose effect on galactose operon expression; its only effect was to stimulate promoter-distal gene expression.

Cyclic AMP↗
PubMed1981

Isolation and characterization of an Escherichia coli mutant affected in the regulation of adenylate cyclase.

A mutant, cyaR1, affecting regulation of adenylate cyclase expression or activity is described. It was obtained as a thermoresistant revertant of a strain harboring a thermosensitive transcription termination factor, rho (rho-15). This mutant failed to synthesize adenosine 3',5'-phosphate and exhibited a carbohydrate-negative phenotype. A secondary mutation at the crp locus (crpC) restored the ability of the mutant to synthesize adenosine 3',5'-phosphate, enabled the expression of catabolite-sensitive operons, and conferred on the strain an extreme sensitivity to catabolite repression. In addition, we showed that the crpC mutation restored the pleiotropic carbohydrate-positive phenotype even in a delta cya background. We interpret this to mean that the adenosine 3',5'-phosphate receptor protein regulates negatively either the activity or synthesis of adenylate cyclase and that the cyaR1 mutation is either in a regulatory protein or a regulatory site of adenylate cyclase.

Adenylyl Cyclases↗
PubMed1980

Volunteers boost spirits of elderly.

Elderly ambulatory patients believed that the hospital staff was too busy to be bothered with the nonmedical problems they had to face in their daily lives.

Continuity of Patient Care↗
PubMed1980

The effect of urea on catabolite sensitive operons in Escherichia coli K 12.

Low concentrations of urea specifically inhibit the expression of catabolite sensitive genes (the lactose, galactose and maltose operons and the tryptophanase gene). This inhibition depends upon growth conditions, i.e. carbon source and temperature. The main effect of urea is exerted at the level of transcription initiation. However an additional inhibitory effect is observed on the decay and expression of the beta-galactosidase messenger. In a strain harboring the UV5 mutation in the lactose promoter, the effect at the level of transcription is relieved while the effect on the decay and the expression of the beta-galactosidase messenger remains the same. Just like the extreme physiological catabolite repression, the urea effect occurs even in a cya delta strain and is not antagonized by addition of adenosine 3'-5' cyclic monophosphate.

Dose-Response Relationship, Drug↗