TY - JOUR A1 - Scheer, Ulrich A1 - Dabauvalle, Marie-Christine A1 - Merkert, Hilde A1 - Benavente, Ricardo T1 - The nuclear envelope and the organization of the pore complexes N2 - No abstract available Y1 - 1988 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-34275 ER - TY - JOUR A1 - Franke, Werner W. A1 - Scheer, Ulrich A1 - Krohne, Georg A1 - Jarasch, Ernst-Dieter T1 - The nuclear envelope and the architecture of the nuclear periphery N2 - No abstract available Y1 - 1981 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33108 ER - TY - JOUR A1 - Krohne, Georg A1 - Franke, Werner W. A1 - Scheer, Ulrich T1 - The major polypeptides of the nuclear pore complex N2 - Nuclear envelopes of maturing oocytes of various amphibia contain an unusually high number of pore complexes in very close packing. Consequently, nuclear envelopes , which can be manually isolated in great purity, provide a remarkable enrichment of nuclear pore complex material, relative to membranous and other interporous structures. When the polypeptides of nuclear envelopes isolated from oocytes of Xenopl/s la evis and Triturus alpestris are examined by gel electrophoresis, visualized either by staining with Coomassie blue or by radiotluorography after in vitro reaction with [3H]dansyl chloride , a characteristic pattern is obtained (10 major and 15 minor bands). This polypeptide pattern is radically different from that of the nuclear contents isolated from the same cell. Extraction of the nuclear envelope with high salt concentrations and moderateIy ac tive detergents such as Triton X- 100 results in the removal of membrane material but leaves most of the non-membranous structure of the pore complexes. The dry weight of the pore complex (about 0.2 femtograms) remains essentially unchanged during such extractions as measured by quantitative electron microscopy . The extracted preparations which are highly enriched in nuclear pore complex material contain only two major polypeptide components with apparent molecular weights of 150000 and 73000. Components of such an electrophoretic mobility are not present as major bands , if at all , in nuclear contents extracted in the same way. lt is concluded that these two polypeptides are the major constituent protein(s) of the oocyte nuclear pore complex and are specific for this structure. When nuclear envelopes are isolated from rat liver and extracted with high salt buffers and Triton X- 100 similar bands are predominant, but two additional major components of molecular weights of 78000 and 66000 are also recognized. When the rat liver nuclear membranes are further subfractionated material enriched in the 66000 molecular weight component can be separated from the membrane material, indicating that this is relatively loosely associated material , probably a part of the nuclear matrix . The results suggest that the nuclear pore complex is not only a characteristic ubiquitous structure but also contains similar, if not identical , skeletal proteins that are remarkably re sistant to drastic changes of ionic strength as weil as to treatments with detergents and thiol reagents. Y1 - 1978 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33078 ER - TY - JOUR A1 - Weisenberger, Dieter A1 - Scheer, Ulrich A1 - Benavente, Ricardo T1 - The DNA topoisomerase I inhibitor camptothecin blocks postmitotic reformation of nucleoli in mammmalian cells N2 - No abstract available KW - Cytologie KW - Nucleolus-DNA KW - opoisomerase I KW - camptothecin KW - mitosis Y1 - 1993 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-41434 ER - TY - JOUR A1 - Reinhard, Matthias A1 - Halbrügge, Maria A1 - Scheer, Ulrich A1 - Wiegand, Christiane A1 - Jockusch, Brigitte M. A1 - Walter, Ulrich T1 - The 46/50 kDa phosphoprotein VASP purified from human platelets is a novel protein associated with actin filaments and focal contacts N2 - Vasoactive agents which elevate either cGMP or cAMP inhibit platelet activation by pathways sharing at least one component, the 46/50 kDa vasodilator-stimulated phosphoprotein (V ASP). V ASP is stoichiometrically phosphorylated by both cGMP-dependent and cAMPdependent protein kinases in intact human platelets, and its phosphorylation correlates very well with platelet inhibition caused by cGMP- and cAMP-elevating agents. Here we report that in human platelets spread on glass, V ASP is associated predominantly with the distal parts of radial micro filament bundles and with microfilaments outlining the periphery, whereas less V ASP is associated with a central microfilamentous ring. V ASP is also detectable in a variety of different cell types including fibroblasts and epithelial cells. In fibroblasts, V ASP is concentrated at focal contact areas, along microfilament bundles (stress fibres) in a punctate pattern, in the periphery of protruding lamellae, and is phosphorylated by cGMP- and cAMP-dependent protein kinases in response to appropriate stimuli. Evidence for the direct binding of V ASP to F -actin is also presented. The data demonstrate that V ASP is a novel phosphoprotein associated with actin filaments and focal contact areas, i.e. transmembrane junctions between microfilaments and the extracellular matrix. KW - cAMP / cGMP / cytoskeleton / phosphorylation / protein kinase Y1 - 1992 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-34246 ER - TY - JOUR A1 - Scheer, Ulrich T1 - Structure of lampbrush chromosome loops during different states of transcriptional activity as visualized in the presence of physiological salt concentrations N2 - Lampbrush chromosomes of amphibian oocytes were isolated in the presence of near-physiological salt concentrations, to preserve their native state, and studied by electron microscopy of ultrathin s~dions. The transcriptional state of the lampbrush chromosomes was experimentally modulated by incubating the oocytes for various time periods in medium containing actinomycin D. The observations show that the structure of the lateral loops changes rapidly in response to alterations in transcriptional activity. During decreasing transcriptional activity and reduced packing density of transcripts, the chromatin axis first condensed into nucleosomes and then into an approximately 30 nm thick higher order chromatin fiber. Packaging of the loop axis into supranucleosomal structures may contribute to the foreshortening and retraction of the loops observed during inhibition of transcription and in later stages of meiotic prophase. The increasing packing density of the DNA during the retraction process of the loops could also be visualized by immunofluorescence microscopy using antibodies to DNA. The dependence of the loop chromatin structure on transcriptional activity is discussed in relation to current views of mechanisms involved in gene activation. KW - lampbrush chromosomes KW - chromatin structure KW - electron microscopy KW - immunofluorescence microscopy KW - DNA antibodies Y1 - 1987 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-39304 ER - TY - JOUR A1 - Trendelenburg, Michael F. A1 - Scheer, Ulrich A1 - Franke, W. W. T1 - Structural organization of the transcription of ribosomal DNA in oocytes of the house cricket N2 - No abstract available Y1 - 1973 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-33113 ER - TY - JOUR A1 - Scheer, Ulrich T1 - Structural organization of spacer chromatin between transcribed ribosomal RNA genes in amphibian oocytes N2 - Transcribed nucleolar chomatin, including the spacer regions interspersed between the rRNA genes, is different from the bulk of nontranscribed chromatin in that the DNA of these regions appears to be in an extended (B) conformation when examined by electron microscopy. The possibility that this may reflect artificial unfolding of nucleosomes during incubation in very low salt buffers as routinely used in such spread preparations has been examined by studying the influence of various ion concentrations on nucleolar chromatin structure. Amplified nucleolar chromatin of amphibian oocytes (Xenopus laevis, Pleurodeles waltlii, Triturus cristatus) was spread in various concentrations of NaCl (range 0 to 20 mM). Below 1 mM salt spacer chromatin frequently revealed a variable number of irregularly shaped beads, whereas above this concentration the chromatin axis appeared uniformly smooth. At all salt concentrations studied, however, the length distribution of spacer and gene regions was identical. Preparations fixed with glutaraldehyde instead of formaldehyde, or unftxed preparations, were indistinguishable in this respect. The observations indicate that (i) rDNA spacer regions are not compacted into nucleosomal particles and into supranucleosomal structures when visualized at chromatin stabilizing salt concentrations (e.g., 20 mM NaCl), and (ii) spacer DNA is covered by a uniform layer of proteins of unknown nature which, at very low salt concentrations (below 1 mM NaCl), can artificially give rise to the appearance of small granular particles of approximately nucleosome-like sizes. These particles, however, are different from nucleosomes in that they do not foreshorten the associated spacer DNA. The data support the concept of an altered nucleohistone conformation not only in transcribed chromatin but also in the vicinity of transcriptional events. KW - Cytologie KW - Chromatin structure KW - rDNA KW - amphibian oocytes Y1 - 1980 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-41057 ER - TY - JOUR A1 - Scheer, Ulrich A1 - Sommerville, J. T1 - Structural organization of nascent transcripts and hnRNA molecules in amphibian oocytes N2 - Comparisons ofrelative lengths oflampbrush loops, nascent RNP transcripts and hnRNA molecules from oocytes of amphibia with different C-values show that there is an increasing trend in loop, and transcriptional unit, length with increase in genome size but no increasing trend with respect to RN A contour length.The formation of duplex regions and circles in RNP fibrils indicates that RNA processing may occur within the nascent fibrils. The hnRNA molecules from oocytes of the various amphibia readily form intermolecular duplex structures. These complementary sequences have a low kinetic complexity and are transcribed from highly repetitive sequences distributed throughout the genome. Their possible function is considered. Y1 - 1981 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-39765 ER - TY - JOUR A1 - Franke, Werner W. A1 - Scheer, Ulrich T1 - Structural details of dictyosomal pores N2 - Structural details of the dictyosomal pores in several plant cell types are described from tangential and cross sections of Golgi cisternae. Frequency distributions of the sizes of such Golgi pores are given and compared with the corresponding values of nuclear pores in the same cells. Golgi pore inner diameters are less homogeneously distributed and can be as small as 100 A or less. They are not simply cisterna I holes, but are often associated with centrally located electron dense granules or rods and with inner pore filaments. This organization, which is very common in dictyosomal pores in plant and animal cells, has some similarities with the structural architecture of nuclear envelope and annulate lamellar pore complexes. The particulate material associated with the dictyosomal pores shows spatial and structural relationship to cytoplasmic ribosomes. Possible modes of Golgi pore formation and some consequences of these observations for interpretation of nuclear pore structures are discussed. Y1 - 1972 U6 - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-32155 ER -