TY - JOUR A1 - Acker, Helmut A1 - Huckstorf, Christine A1 - Sauer, Heinrich A1 - Streller, Tino A1 - Wartenberg, Maria T1 - Deciphering the oxygen sensing pathway by microscopy Y1 - 2004 ER - TY - JOUR A1 - Albrecht, Tanja A1 - Haebel, Sophie A1 - Koch, Anke A1 - Krause, Ulrike A1 - Eckermann, Nora A1 - Steup, Martin T1 - Yeast glycogenin (Glg2p) produced in Escherichia coli is simultaneously glucosylated at two vicinal tyrosin residues but results in a reduced bacterial glycogen accumulation N2 - Saccharomyces cerevisiae possesses two glycogenin isoforms (designated as Glg1p and Glg2p) that both contain a conserved tyrosine residue, Tyr232. However, Glg2p possesses an additional tyrosine residue, Tyr230 and therefore two potential autoglucosylation sites. Glucosylation of Glg2p was studied using both matrix-assisted laser desorption ionization and electrospray quadrupole time of flight mass spectrometry. Glg2p, carrying a C-terminal (His(6)) tag, was produced in Escherichia coli and purified. By tryptic digestion and reversed phase chromatography a peptide (residues 219-246 of the complete Glg2p sequence) was isolated that contained 4-25 glucosyl residues. Following incubation of Glg2p with UDPglucose, more than 36 glucosyl residues were covalently bound to this peptide. Using a combination of cyanogen bromide cleavage of the protein backbone, enzymatic hydrolysis of glycosidic bonds and reversed phase chromatography, mono- and diglucosylated peptides having the sequence PNYGYQSSPAM were generated. MS/MS spectra revealed that glucosyl residues were attached to both Tyr232 and Tyr230 within the same peptide. The formation of the highly glucosylated eukaryotic Glg2p did not favour the bacterial glycogen accumulation. Under various experimental conditions Glg2p-producing cells accumulated approximately 30% less glycogen than a control transformed with a Glg2p lacking plasmid. The size distribution of the glycogen and extractable activities of several glycogen-related enzymes were essentially unchanged. As revealed by high performance anion exchange chromatography, the intracellular maltooligosaccharide pattern of the bacterial cells expressing the functional eukaryotic transgene was significantly altered. Thus, the eukaryotic glycogenin appears to be incompatible with the bacterial initiation of glycogen biosynthesis Y1 - 2004 ER - TY - JOUR A1 - Ale-Agha, Nosratollah A1 - Bolay, Adrien A1 - Braun, Uwe A1 - Jage, Horst A1 - Kummer, Volker A1 - Lebeda, Ales A1 - Piatek, Marcin A1 - Shin, Hyeon-Dong A1 - Zimmermannova-Pastircakova, Katarina T1 - Erysiphe catalpae and E. elevata in Europe Y1 - 2004 ER - TY - JOUR A1 - Anders, Kenneth A1 - Beier, Wolfgang A1 - Brunk, Ingo A1 - Burkart, Bettina A1 - Mrzljak, Anders A1 - Oehlschläger, Susanne T1 - Freie Sukzession und Offenlandmanagement Y1 - 2004 SN - 3-540-22449-1 ER - TY - JOUR A1 - Anders, Kenneth A1 - Mrzljak, Jadranka A1 - Wallschläger, Hans-Dieter A1 - Wiegleb, Gerhard T1 - Handbuch Offenlandmanagement am Beispiel ehemaliger und in Nutzung befindlicher Truppenübungsplätze Y1 - 2004 SN - 3-540-22449-1 PB - Springer CY - Berlin ER - TY - JOUR A1 - Anders, Kenneth A1 - Prochnow, Annette A1 - Schlauderer, Ralf A1 - Wiegleb, Gerhard T1 - Die Szenario-Methode als Instrument der Naturschutzplanung im Offenland Y1 - 2004 SN - 3-540-22449-1 ER - TY - JOUR A1 - Baumann, Otto T1 - Konventionelle Fluoreszenzmikroskopie : Theorie und Anwendungsmöglichkeiten Y1 - 2004 ER - TY - JOUR A1 - Baumann, Otto T1 - Spatial pattern of nonmuscle myosin-II distribution during the development of the Drosophila compound eye and implications for retinal morphogenesis N2 - Nonmuscle myosin-II is a motor protein that drives cell movement and changes in cell shape during tissue and organ development. This study has determined he dynamic changes in myosin-II distribution during Drosophila compound eye morphogenesis. In photoreceptor neurons, myosin-II is undetectable at the apical domain throughout the first half of pupal life, at which time this membrane domain is involuted into the epithelium and progresses toward the retinal floor. Myosin-II is deployed at the apical surface at about 60% of pupal development, once the developing rhabdomeres reach the retinal floor. Subsequently, myosin-II becomes restricted to two stripes at the sides of the developing rhabdomere, adopting its final position within the visual cells R1-6; here, myosin-II is associated with a set of actin filaments that extend alongside the rhabdomeres. At the midpupal stage, myosin-II is also incorporated into stress-fiber-like arrays within the basal endfeet of the pigment cells that then change their shape. This spatiotemporal pattern of myosin- II localization and the morphological defects observed in the eyes of a myosin-II mutant suggest that the myosin-II/F- actin system is involved in the alignment of the rhabdomeres within the retina and in the flattening of the retinal floor. The observation that the myosin-II/F-actin arrays are incomplete or disorganized in R7/R8 and in rhodopsin-1-null R1-6 suggests further that the establishment and stability of this cytoskeletal system depend on rhodopsin-1 expression. (C) 2004 Elsevier Inc. All rights reserved Y1 - 2004 ER - TY - JOUR A1 - Baumann, Otto A1 - Kühnel, Dana A1 - Dames, Petra A1 - Walz, Bernd T1 - Dopaminergic and serotonergic innervation of cockroach salivary glands : distribution and morphology of synapses and release sites N2 - The paired salivary glands in the cockroach are composed of acini with ion-transporting peripheral P-cells and protein-secreting central C-cells, and a duct system for the modification of the primary saliva. Secretory activity is controlled by serotonergic and dopaminergic neurons, whose axons form a dense plexus on the glands. The spatial relationship of release sites for serotonin and dopamine to the various cell types was determined by anti-synapsin immunofluorescence confocal microscopy and electron microscopy. Every C-cell apparently has only serotonergic synapses on its surface. Serotonergic and dopaminergic fibres on the acini have their release zones at a distance of similar to0.5 mum from the P-cells. Nerves between acinar lobules may serve as neurohaemal organs and contain abundant dopaminergic and few serotonergic release sites. Some dopaminergic and serotonergic release sites reside in the duct epithelium, the former throughout the duct system, the latter only in segments next to acini. These findings are consistent with the view that C-cells respond exclusively to serotonin, P-cells to serotonin and dopamine, and most duct cells only to dopamine. Moreover, the data suggest that C-cells are stimulated by serotonin released close to their surface, whereas P-cells and most duct cells are exposed to serotonin/dopamine liberated at some distance Y1 - 2004 ER - TY - JOUR A1 - Beatham, Jane L. A1 - Middleton, A. A1 - Romero, Rosario A1 - VanderVen, Peter F. M. A1 - Blanco, Gonzalo T1 - Functional characterisation of the Ky protein Y1 - 2004 SN - 0960-8966 ER -