PubMed Health⌕ Search

Biomedical subjects

C Rossier

Publications and source records attributed to C Rossier.

65 records · Page 4Linked to original sources
PubMed1985

Genetic analysis of transformation in a microconidiating strain of Neurospora crassa.

We have characterized Neurospora crassa transformants obtained with plasmid pDV1001 bearing the cloned catabolic dehydroquinase (qa-2+) gene (Hughes et al. 1983a) and fluffy 268 host strain producing only uninucleate microconidia allowing to isolate individual transformation products. The percentage of transformed nuclei in the mycelium and their stability were determined by genetic analysis of microconidia produced on selective or non-selective medium. About half of the transformants originating from mycelial spheroplasts were apparently homokaryotic. Catabolic dehydroquinase activity was in agreement with the proportion of transformed nuclei. The DNAs from four transformants analyzed by Southern hybridization showed restriction fragments expected for integration of pDV1001 into genomic DNA by non-homologous recombination. No plasmids could be rescued from the undigested DNAs of the transformants by transformation of E. coli. One transformant, fl268-6, was unstable and generated a high proportion of segregants. Plasmid pDV1001 sequences were absent in their DNA. Colonies originating from microconidia of strain fl268-6 on selective plates often lost the transformed character. These results suggest that instability in this transformant is due to the loss of integrated plasmid sequences during vegetative growth.

DNA, Fungal↗
PubMed1983

Detection and regulation of the mRNA for the inhibitor of extracellular cAMP phosphodiesterase of Dictyostelium discoideum.

The inhibitor of the cAMP phosphodiesterase of Dictyostelium discoideum is a cysteine-rich glycoprotein, which binds to the enzyme and inactivates it. When the inhibitor is removed, enzymatic activity is restored. Following translation in vitro of RNA from developing cells and immunoprecipitation with anti-inhibitor serum, newly synthesized inhibitor can be detected by sodium dodecylsulfate/polyacrylamide gel electrophoresis and fluorography. The inhibitor can be labeled using [35S]cysteine but not [35S]methionine, in agreement with the previously determined amino acid composition, and can be detected after cell-free translation only if it has been previously acetylated. Purified native inhibitor blocks immunoprecipitation of the inhibitor polypeptide synthesized in vitro. No inhibitor mRNA was detected in growing cells. Translatable mRNA was present 2 h after the beginning of starvation, reached a maximal level after 3 h, and decreased thereafter. Addition of 1 mM cAMP at the beginning of starvation delayed the appearance of translatable inhibitor mRNA. In the presence of 5 microM adenosine cyclic-3',5'-phosphorothioate, a slowly hydrolyzed cAMP analogue, no translatable mRNA could be detected. Following removal of the analogue, the mRNA appeared within one hour and inhibitor was secreted after another hour.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1982

A fragment of Dictyostelium discoideum genomic DNA that complements the URA1 mutation of Saccharomyces cerivisiae.

A strain of Saccharomyces cerivisiae carrying a mutation in the URA1 gene was transformed with fragments of Dictyostelium DNA inserted into a plasmid capable of replication in E. coli or yeast. Rare prototrophic colonies were recovered that all contained the parent plasmid and an insert of Dictyostelium DNA. Resistance to the antibiotic G418, a function coded by the same plasmid, was also expressed in the prototrophs. Plasmids recovered from the prototrophic yeast could be used to transform E. coli. The E. coli transformants harbored plasmids capable of transforming yeast URA1 mutants to prototrophy. No complementation of the E. coli pyrD mutation, which corresponds to URA1, occurred. Southern blot analysis revealed that the insert of Dictyostelium DNA contained a unique sequence of 1700 base pairs and a repetitive one of 1000 base pairs. Subcloning experiments showed that only the unique sequence was required for complementation, which is independent of the orientation of the Dictyostelium sequence in the plasmid. The repetitive fragment was not linked to the unique sequence in the genome and was probably an artifact of the ligation procedure. The unique sequence hybridized to a Dictyostelium polyA+ RNA species of 1200-1300 bases.

Chromosome Mapping↗
PubMed1981

Folate deaminase and cyclic AMP phosphodiesterase in Dictyostelium discoideum: their regulation by extracellular cyclic AMP and folic acid.

Cyclic AMP and folic acid act as chemotactic factors in Dictyostelium discoideum. Both agents, when applied extracellularly, also control cell development from the growth stage to the acquisition of aggregation competence. Cyclic AMP phosphodiesterase and folate deaminase are extracellular enzymes whose activity is regulated during early differentiation of D. discoideum cells. The two enzymes help control the extracellular levels of cyclic AMP and folic acid. The substrates cyclic AMP and folic acid each increase the extracellular activity of folate deaminase as well as phosphodiesterase. The specificity of extracellular phosphodiesterase regulation by cyclic AMP indicates that the effect is mediated by specific cyclic AMP receptors rather than the catalytic site of cell surface phosphodiesterase. To some extent cyclic AMP and folic acid are interchangeable with respect to regulating differentiation and enhancing enzymatic inactivation of intercellular signals. Thus the two extracellular signals may share a common cellular pathway of signal transduction. The regulation of folate deaminase and phosphodiesterase by folic acid does not always parallel the folic acid effects on development. Pulses of folic acid stimulate development of aggregation competence, whereas a continuous flux inhibits. In contrast, either continuous flux or pulses of folic acid increase the deaminase and phosphodiesterase activities.

3',5'-Cyclic-AMP Phosphodiesterases↗
PubMed1979

Action of a slowly hydrolysable cyclic AMP analogue on developing cells of Dictyostelium discoideum.

Adenosine 3',5'-cyclic phosphorothioate (cAMP-S) is a cyclic AMP (cAMP) analogue which is only slowly hydrolysed by phosphodiesterases of Dictyostelium discoideum. The affinity of cAMP-S to cAMP receptors at the cell surface is only one order of magnitude lower than that of cAMP. cAMP-S can replace cAMP as a stimulant with respect to all receptor-mediated responses tested, including chemotaxis and the induction of cAMP pulses. cAMP-S does not affect growth of D. discoideum but it blocks cell aggregation at a uniform concentration of 5 x 10(-7) M in agar plate cultures of strain NC-4 as well as its axenically growing derivative, Ax-2. Another wild-type strain of D. discoideum, v-12, is able to aggregate on agar plates supplemented with 1 mM cAMP-S. The development of Polysphondylium pallidum and P. violaceum is also highly cAMP-S resistant. In Ax-2 both differentiation from the growth phase to the aggregation-competent stage and chemotaxis are cAMP-S sensitive, whereas in v-12 only chemotaxis is inhibited. v-12 can still form streams of cohering cells and fruiting bodies when chemotaxis is inhibited by cAMP-S. Whereas cAMP induces differentiation into stalk cells at concentrations of 10(-3) or 10(-4) M, cAMP-S has the same effect in strain v-12 at the much lower concentration of 10(-6) M.

Chemotaxis↗
PubMed1976

Changes of some enzymatic activities in iodoacetate-treated microconidiating cultures of Neurospora crassa.

In iodoacetate-treated microconidating cultures of Neurospora crassa, mycelial yield, sucrose consumption and ethanol production are reduced. The specific activity of glyceraldehyde-3-phosphate dehydrogenase is sharply decreased while the specific activities of glucose-6-phosphate dehydrogenase and of 6-phosphogluconate dehydrogenase are stimulated. A polyphenoloxidase is induced in the microconidiating cultures.

Catechol Oxidase↗
PubMedDate not supplied

No detected mutations in the genes for the amyloid precursor protein and presenilins 1 and 2 in a swiss early-onset Alzheimer's disease family with a dominant mode of inheritance.

Mutations have been found in more than a hundred early-onset families with Alzheimer's disease (AD) in the genes for the amyloid precursor protein, presenilin 1 and presenilin 2. The object of our investigation was to identify if these mutations or novel ones were operating in a Swiss early-onset AD family (mean age of onset: 53.3 years) with 7 members available, all neuropathologically confirmed. No known or new mutations were detected. Thus, our data support the existence of a yet unknown mutation, or other genes, contributing to familial early-onset AD. CopyrightCopyright 1999S.KargerAG,Basel

Adult↗