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Biomedical subjects

Stefan Lorenz

Publications and source records attributed to Stefan Lorenz.

3 recordsLinked to original sources

Experimental demonstration of continuous variable quantum erasing.

We experimentally demonstrate the concept of continuous variable quantum erasing. The amplitude quadrature of the signal state is labeled to another state via a quantum nondemolition interaction, leading to a large uncertainty in the determination of the phase quadrature due to the inextricable complementarity of the two observables. We show that by erasing the amplitude quadrature information we are able to recover the phase quadrature information of the signal state.

Journal Article↗

Cyclin D-knockout uncouples developmental progression from sugar availability.

Multicellular organisms need to modulate proliferation and differentiation in response to external conditions. An important role in these processes plays the mitogen-stimulated induction of cyclin D (cycD) gene expression. D-type cyclins have been identified as the crucial intracellular sensors for cell-cycle regulation in all eukaryotes. However, cycD deletions have been found to cause specific phenotypic alterations in animals but not yet in plants. An insertional mutation of a so far uncharacterized Arabidopsis cycD gene did not alter the plant phenotype. To gain new insights into CycD function of land plants, we generated targeted cycD gene knockouts in the moss Physcomitrella patens and observed a surprisingly limited disruption phenotype. While wild-type plants reacted to exogenous glucose sources with prolonged growth of juvenile stages and retarded differentiation, cycD knockouts exhibited developmental progression independent of sugar supply. On the other hand, growth rate, cell sizes or plant size were not affected. Thus, we conclude that Physcomitrella CycD might not be essential for cell-cycle regulation but is important for coupling the developmental progression to nutrient availability.

Blotting, Southern↗

Escherichia coli glutamyl-tRNA reductase. Trapping the thioester intermediate.

In the first step of tetrapyrrole biosynthesis in Escherichia coli, glutamyl-tRNA reductase (GluTR, encoded by hemA) catalyzes the NADPH-dependent reduction of glutamyl-tRNA to glutamate-1-semialdehyde. Soluble homodimeric E. coli GluTR was made by co-expressing the hemA gene and the chaperone genes dnaJK and grpE. During Mg(2+)-stimulated catalysis, the reactive sulfhydryl group of Cys-50 in the E. coli enzyme attacks the alpha-carbonyl group of the tRNA-bound glutamate. The resulting thioester intermediate was trapped and detected by autoradiography. In the presence of NADPH, the end product, glutamate-1-semialdehyde, is formed. In the absence of NADPH, E. coli GluTR exhibited substrate esterase activity. The in vitro synthesized unmodified glutamyl-tRNA was an acceptable substrate for E. coli GluTR. Eight 5-aminolevulinic acid auxotrophic E. coli hemA mutants were genetically selected, and the corresponding mutations were determined. Most of the recombinant purified mutant GluTR enzymes lacked detectable activity. Based on the Methanopyrus kandleri GluTR structure, the positions of the amino acid exchanges are close to the catalytic domain (G7D, E114K, R314C, S22L/S164F, G44C/S105N/A326T, G106N, S145F). Only GluTR G191D (affected in NADPH binding) revealed esterase but no reductase activity.

Aldehyde Oxidoreductases↗