@article{ScheerMessnerHazanetal.1987,
  author    = {Scheer, Ulrich and Messner, Karin and Hazan, Rachel and Raska, Ivan and Hansmann, Paul and Falk, Heinz and Spiess, Eberhard and Franke, Werner W.},
  title     = {High sensitivity immunolocalization of double and single-stranded DNA by a monoclonal antibody},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41063},
  year      = {1987},
  abstract  = {A monoclonal antibody (AK 30-10) is described which specifically reacts with DNA both in double and single-stranded forms but not with other molecules and structures, including deoxyribonucleotides and RNAs. When used in immunocytochemical experiments on tissue sections and permeabilized cultured cells, this antibody detects DNA-containing structures, even when the DNA is present in very small amounts. Examples of high resolution detection include the DNA present in amplified extrachromosomal nucleoli, chromomeres of lampbrush chromosomes, mitochondria, chloroplasts and mycoplasmal particles. In immunoelectron microscopy using the immunogold technique, the DNA was localized in distinct substructures such as the "fibrillar centers" of nucleoli and certain stromal centers in chloroplasts. The antibody also reacts with DNA of chromatin of living cells, as shown by microinjection into cultured mitotic cells and into nuclei of amphibian oocytes. The potential value and the limitations of immunocytochemical DNA detection are discussed.},
  subject      = {Cytologie},
  language  = {en}
}
@article{HuegleScheerFranke1985,
  author    = {H{\"u}gle, Barbara and Scheer, Ulrich and Franke, Werner W.},
  title     = {Ribocharin: a nuclear M\(_r\) 40,000 protein specific to precursor particles of the large ribosomal subunit},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41169},
  year      = {1985},
  abstract  = {Using a monoclonal antibody (No-194) we have identified, in Xenopus laevis and other amphibia, an acidic protein of M, 40,000 (ribocharin) which is specifically associated with the granular component of the nucleolus and nucleoplasmic 65S particles. These particles contain the nuclear 28S rRNA and apparently represent the precursor to the large ribosomal subunit in nucleocytoplasmic transit. By immunoelectron microscopy ribocharin has been localized in the granular component of the nucleolus and in interchromatin granules. During mitosis ribocharin-containing particles are associated with surfaces of chromosomes and are recollected in the reconstituting nucleoli in late telophase. We suggest that ribocharin is a specific component of precursor particles of the large ribosomal subunit, which dissociates from the 65S particle before passage through the nuclear envelope, and is reutilized in ribosome biogenesis.},
  language  = {en}
}
@article{HuegleHazanScheeretal.1985,
  author    = {H{\"u}gle, Barbara and Hazan, Rachel and Scheer, Ulrich and Franke, Werner W.},
  title     = {Localization of ribosomal protein S1 in the granular component of the interphase nucleolus and its distribution during mitosis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39695},
  year      = {1985},
  abstract  = {Using antibodies to various nucleolar and ribosomal proteins, we define, by immunolocalization in situ, the distribution of nucleolar proteins in the different morphological nucleolar subcompartments. In the present study we describe the nucleolar localization of a specific ribosomal protein (51) by immunofluorescence and immunoelectron microscopy using a monoclonal antibody (R5 1-105). In immunoblotting experiments, this antibody reacts specifically with the largest and most acidic protein of the small ribosomal subunit (51) and shows wide interspecies cross-reactivity from amphibia to man. Beside its localization in cytoplasmic ribosomes, this protein is found to be specifically localized in the granular component of the nucleolus and in distinct granular aggregates scattered over the nucleoplasm. This indicates that ribosomal protein 51, in contrast to reports on other ribosomal proteins, is not bound to nascent pre-rRNA transcripts but attaches to preribosomes at later stages of rRNA processing and maturation. This protein is not detected in the residual nucleolar structures of cells inactive in rRNA synthesis such as amphibian and avian erythrocytes. During mitosis, the nucleolar material containing ribosomal protein 51 undergoes a remarkable transition and shows a distribution distinct from that of several other nucleolar proteins. In prophase, the nucleolus disintegrates and protein 51 appears in numerous small granules scattered throughout the prophase nucleus. During metaphase and anaphase, a considerable amount of this protein is found in association with the surfaces of all chromosomes and finely dispersed in the cell plasm. In telophase, protein 51-containing material reaccumulates in granular particles in the nucleoplasm of the newly formed nuclei and, finally, in the re-forming nucleoli. These observations indicate that the nucleolus-derived particles containing ribosomal protein 51 are different from cytoplasmic ribosomes and, in the living cell, are selectively recollected after mitosis into the newly formed nuclei and translocated into a specific nucleolar subcompartment, i.e ., the granular component. The nucleolar location of ribosomal protein 51 and its rearrangement du'ring mitosis is discussed in relation to the distribution of other nucleolar proteins.},
  subject      = {Cytologie},
  language  = {en}
}
@article{ScheerSchmidtZachmannHuegleetal.1984,
  author    = {Scheer, Ulrich and Schmidt-Zachmann, Marion S. and H{\"u}gle, Barbara and Franke, Werner W.},
  title     = {Identification and localization of a novel nucleolar protein of a high molecular weight by a monoclonal antibody},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39786},
  year      = {1984},
  abstract  = {A monoclonal murine antibody (No-I 14) is described which reacts specifically with a polypeptide of molecular weight (M,) 180000 present in low-speed nuclear pellets from oocytes and somatic cells of Xenopus laevis and X. borealis and in isolated amplified nucleoli. Two-dimensional gel electrophoresis has revealed the acidic nature of this polypeptide (isoelectric at pH of ca 4.2 in the presence of 9.5 M urea). A relatively large proportion of the protein is extracted at elevated ionic strength( i.e., at 0.4-0.5 M alkali salt) in a form sedimenting at approx. 7-8S , compatible with a monomeric state. It is also extracted by digestion with RNase but not with DNase. In immunofluorescence microscopy, antibody No-114 stains intensely nucleoli of oocytes and all somatic cells examined , including the residual nucleolar structure of Xenopus erythrocytes which are transcriptionally inactive. During mitosis the antigen does not remain associated with the nucleolar organizer regions (NOR) of chromosomes but is released and dispersed over the cytoplasm until telophase when it re-associates with the reforming interphase nucleoli. At higher resolution the immunofluorescent region is often resolved into a number of distinct subnucleolar components of varied size and shape. Immunoelectron microscopy using colloidal gold-coupled secondary antibodies reveals that the M, 180000 protein is confined to the dense fibrillar component of the nucleolus. This conclusion is also supported by its localization in the fibrillar part of segregated nucleoli of cells treated with actinomycin D. We conclude that nucleoli contain a prominent protein of M, 180000 which contributes to the general structure of the dense fibrillar component of the interphase nucleolus , independent of its specific transcriptional activity.},
  language  = {en}
}
@article{ScheerHinssenFrankeetal.1984,
  author    = {Scheer, Ulrich and Hinssen, Horst and Franke, Werner W. and Jockusch, Brigitte M.},
  title     = {Microinjection of actin-binding proteins and actin antibodies demonstrates involvement of nuclear actin in transcription of lampbrush chromosomes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39706},
  year      = {1984},
  abstract  = {Nuclei of amphibian oocytes contain large amounts of actin, mostly in unpolymerized or short-polymer form. When antibodies to actin or actin-binding proteins (fragmin and the actin modulator from mammalian smooth muscle) are injected into nuclei of living oocytes of Pleurodeles waltlii, transcription of the lampbrush chromosomes, but not of the rRNA genes, is inhibited. When transcription is repressed by drugs or RNA is digested by microinjection of RNAase into oocyte nuclei, an extensive meshwork of actin filament bundles is seen in association with the isolated lampbrush chromosomes. These observations indicate a close relationship between the state of nuclear actin and transcriptional activity and suggest that nuclear actin may be involved in transcriptional events concerning protein-coding genes.},
  language  = {en}
}
@article{FrankeScheerZentgraf1984,
  author    = {Franke, Werner W. and Scheer, Ulrich and Zentgraf, Hanswalter},
  title     = {Organization of transcriptionally active and inactive chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40588},
  year      = {1984},
  abstract  = {No abstract available},
  subject      = {Deutschland},
  language  = {en}
}
@article{ScheerLanfranchiRoseetal.1983,
  author    = {Scheer, Ulrich and Lanfranchi, Gerolamo and Rose, Kathleen M. and Franke, Werner W. and Ringertz, Nils R.},
  title     = {Migration of rat RNA polymerase I into chick erythrocyte nuclei undergoing reactivation in chick-rat heterokaryons},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33232},
  year      = {1983},
  abstract  = {Transcriptionally inactive chick erythrocyte nudei were reactivated by Sendai virusinduced fusion of erythrocytes with rat L6j1 myoblasts. We used antibodies to trace the appearance of a specific protein engaged in transcription of a defined dass of genes, those coding for rRNA, during reactivation. Using immunofluorescence microscopy, we found increasing amounts of rat RNA polymerase I to appear, during a certain period of time after fusion, in the reforming nudeoli of the chick nudei. Amounts of rat RNA polymerase I sufficient to be detected by immunofluorescence microscopy had accumulated in the newly developed chick nudeoli 72- 190 h after fusion was initiated. This time interval coincides with the time when chick rRNA synthesis can first be detected. The results raise the possibility that during these stages of the reactivation process chick rRNA genes are transcribed by heterologous RNA polymerase I moleeules of rat origin.},
  language  = {en}
}
@article{KleinschmidtScheerDabauvalleetal.1983,
  author    = {Kleinschmidt, J{\"u}rgen A. and Scheer, Ulrich and Dabauvalle, Marie-Christine and Bustin, Michael and Franke, Werner W.},
  title     = {High mobility group proteins of amphibian oocytes: a large storage pool of a soluble high mobility group-1-like protein and involvement in transcriptional events},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33250},
  year      = {1983},
  abstract  = {No abstract available},
  language  = {en}
}
@article{MorenoDiazdelaEspinaFrankeKrohneetal.1982,
  author    = {Moreno-Diaz de la Espina, Susana and Franke, Werner W. and Krohne, Georg and Trendelenburg, Michael F. and Grund, Christine and Scheer, Ulrich},
  title     = {Medusoid fibril bodies: a novel type of nuclear filament of diameter 8 to 12 nm with periodic ultrastructure demonstrated in oocytes of Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-34116},
  year      = {1982},
  abstract  = {No abstract available},
  language  = {en}
}
@incollection{ScheerKleinschmidtFranke1982,
  author    = {Scheer, Ulrich and Kleinschmidt, J{\"u}rgen A. and Franke, Werner W.},
  title     = {Transcriptional and skeletal elements in nucleoli of amphibian oocytes},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40625},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1982},
  abstract  = {No abstract available},
  language  = {en}
}
@article{FrankeScheerKrohneetal.1981,
  author    = {Franke, Werner W. and Scheer, Ulrich and Krohne, Georg and Jarasch, Ernst-Dieter},
  title     = {The nuclear envelope and the architecture of the nuclear periphery},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33108},
  year      = {1981},
  abstract  = {No abstract available},
  language  = {en}
}
@article{FrankeKleinschmidtSpringetal.1981,
  author    = {Franke, Werner W. and Kleinschmidt, J{\"u}rgen A. and Spring, Herbert and Krohne, Georg and Grund, Christine and Trendelenburg, Michael F. and St{\"o}hr, Michael and Scheer, Ulrich},
  title     = {A nucleolar skeleton of protein filaments demonstrated in amplified nucleoli of Xenopus laevis},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33130},
  year      = {1981},
  abstract  = {The amplified, extrachromosomal nucleoli of Xenopus oocytes contain a meshwork of -4-nm-thick filaments, which are densely coiled into higher-order fibrils of diameter 30-40 nm and are resistant to treatment with high- and low-salt concentrations, nucleases (DNase I, pancreatic RNase, micrococcal nuclease), sulfhydryl agents, and various nonionic detergents. This filamentous "skeleton" has been prepared from manually isolated nuclear contents and nucleoli as weil as from nucleoli isolated by fluorescence-activated particle sorting. The nucleolar skeletons are observed in light and electron microscopy and are characterized by ravels of filaments that are especially densely packed in the nucleolar cortex. DNA as weil as RNA are not constituents of this structure, and precursors to ribosomal RNAs are completely removed from the extraction-resistant filaments by treatment with high-salt buffer or RN ase. Fractions of isolated nucleolar skeletons show specific enrichment of an acidic major protein of 145,000 mol wt and an apparent pi value of -6.15, accompanied in some preparations by various amounts of minor proteins. The demonstration of this skeletal structure in "free" extrachromosomal nucleoli excludes the problem of contaminations by nonnucleolar material such as perinucleolar heterochromatin normally encountered in studies of nucleoli from somatic cells. It is suggested that this insoluble protein filament complex forms a skeleton specific to the nucleolus proper that is different from other extraction-resistant components of the nucleus such as matrix and lamina and is involved in the spatial organization of the nucleolar chromatin and its transcriptional products. In studies of the organization of the interphase nucleus, considerable progress has been made in the elucidation of the arrangement of chromatin components and transcriptional products. However, relatively little is known about the composition and function of another category of nuclear structures, the nonnucleoproteinaceous architectural components that are insoluble in solutions of low and high ionic strength, despite numerous studies dedicated to this problem. Such structures include (a) the nuclear envelope and its pore complexes (I, 15, 18, 23, 37, 41), (b) a peripheral layer of insoluble protein ("lamina"; I, 15, 22, 23, 59), (e) certain skeletal proteins related to the chromosome "scaffold" described by Laemmli and coworkers (see references 2 and 3), and (d) ill-defined tangles of fibrillar structures of the nuclear interior that are collectively described as residual "matrix" (6, 21 ; for reviews, see references THE JOURNAL OF CEll BrOlOGY . VOlUME 90 AUGUST 1981 289-299 © The RockefeIler University Press · 0021 -9525/ 81 / 08/ 0289/ 11 \$1 .00 4 and 12). The latter, preparatively},
  language  = {en}
}
@incollection{FrankeScheerZentgrafetal.1980,
  author    = {Franke, Werner W. and Scheer, Ulrich and Zentgraf, Hanswalter and Trendelenburg, Michael F. and M{\"u}ller, U. and Krohne, G. and Spring, H.},
  title     = {Organization of transcribed and nontranscribed chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-40656},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1980},
  abstract  = {No abstract available},
  subject      = {Tumor / Zellteilung},
  language  = {en}
}
@incollection{FrankeScheerSpringetal.1979,
  author    = {Franke, Werner W. and Scheer, Ulrich and Spring, Herbert and Trendelenburg, Michael F. and Zentgraf, Hanswalter},
  title     = {Organization of nucleolar chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39410},
  publisher      = {Universit{\"a}t W{\"u}rzburg},
  year      = {1979},
  abstract  = {No abstract available},
  language  = {en}
}
@article{ZentgrafTrendelenburgSpringetal.1979,
  author    = {Zentgraf, Hanswalter and Trendelenburg, Michael F. and Spring, Herbert and Scheer, Ulrich and Franke, Werner W. and M{\"u}ller, Ulrike and Drury, Kenneth C. and Rungger, Duri},
  title     = {Mitochondrial DNA arranged into chromatin-like structures after injection into amphibian oocyte nuclei},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33174},
  year      = {1979},
  abstract  = {Purified mitochondrial DNA (mitDNA) from ovaries ofXenopus lae vis was injected into the nuclei (germinal vesicles) of large viteUogenic oocytes of the same organism and examined by electron microscopy ofthe spread nuclear contents. Normally located nuclei of untreated oocytes as weil as peripherally translocated nuclei of centrifuged oocytes were used. In addition, oocyte nuclei isolated and incubated under liquid paraffin oil were injected with DNA. The integrity oftranscriptional structures of endogenous chromosomal (Iampbrush chromosomes) and extrachromosomal (nucleoli) genes of the injected nuclei was demonstrated. Microinjected mitDN A was identified as circles of chromatin exhibiting polynucleosome-like organization and a me an contour length of 2.6 J.Lm, corresponding to a compaction ratio of the mitDN A of about 2 : I. This DNA packing ratio is similar to that observed after preparation of various kinds of native chromatin in low salt buffers. The chromatin circles formed from injected mitDNA only very rarely exhibited lateral fibrils suggestive of transcriptional activity. These results suggest that purified mitDNA can be transformed to normally structured chromatin when exposed to oocyte nuclear contents but is rarely , if at all , transcribed in this form and in this environment.},
  language  = {en}
}
@article{FrankeScheer1978,
  author    = {Franke, Werner W. and Scheer, Ulrich},
  title     = {Morphology of transcriptional units at different states of activity},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41363},
  year      = {1978},
  abstract  = {The morphology of two forms of transcription ally active chromatin, the nucleoli and the loops of lampbrush chromosomes, has been examined after fixation in situ or after isolation and dispersion of the material in media of low ionic strengths, using a variety of electron microscopic preparation techniques (e.g. spread preparations with positive or negative staining or without any staining at all, with bright and dark field illumination, with autoradiography, after pretreatment of the chromatin with specific detergents such as Sarkosyl NL-30; transmission and scanning transmission electron microscopy of ultrathin sections). Nucleolar chromatin and chromosomes from oocytes of various amphibia and insects as well as from green algae of the family of the Dasycladaceae were studied in particular detail. The morphology of transcriptional units that are densely packed with lateral ribonucleoprotein fibrils, indicative of great transcriptional activity, was compared with that of chromatin of reduced lateral fibril density, including stages of drug-induced inhibition. The micrographs showed that under conditions which preserve the nucleosomal organization in condensed chromatin studied in parallel, nucleosomes are not recognized in transcriptionally active chromatin. This holds for the transcribed regions as well as for apparently untranscribed (i.e. fibril-free) regions interspersed between ('spacer') and/or adjacent to transcribed genes and for the fibril-free regions within transcriptional units of reduced fibril density. In addition, comparison oflengths of repeating units of isolated rDNA with those observed in spread nucleolar chromatin indicated that this DNA is not foreshortened and packed into nucleosomal structures. Granular particles which were observed, at irregular frequencies and in variable patterns, in some spacer regions, did not result in a proportional shortening of the spacer axis, and were found to be resistant to detergent treatment effective in removing most of the chromatin associated proteins including histones. Thus, these particles behave like RNA polymerases rather than nucleosomes. It is suggested that structural changes from nucleosomal packing to an extended form of DNA are involved in the transcriptional activation of chromatin.},
  language  = {en}
}
@inproceedings{FrankeZentgrafScheer1978,
  author    = {Franke, Werner W. and Zentgraf, Hanswalter and Scheer, Ulrich},
  title     = {Supranucleosomal and non-nucleosomal chromatin configurations},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39447},
  year      = {1978},
  abstract  = {A significant contribution to the understanding of chromatin organization was the d iscovery of the nucleosome as a globular repeating unit of the package of DNA (Hewish and Burgoyne, 1973; Woodcock, 1973; Kornberg, 1974; Olins and Olins, 1974; for review see Oudet et al., 1978 a) . In accord with the original definition and in ag reement with most workers in this field of research we identify a nucleosome as a spheric alor slightly oblate gr anular particle 10-13 nm in diameter, containing about 200 base pairs of DNA and two of each of the four his tones H2a, H2b, H3 and H4. It is this structure in which the bulk of the nuclear chroma tin is organized in most eukaryotic cells, with the exception of the dinofl age llates (Rae and Steele, 1977; dinofl agellate DNA, however, c an be packed into nucleosoma l structures in vitro by addition of the appropriate amounts of histones;the same reference). Although it seems clear from the work reported that condensed and transcriptiona lly inactive chroma tin is contained in nucleosomes as the principle for first order p acking of DNA there are two important questions onto which we are focusing in the present study: ( i ) What is the higher order of p a cking present in - and perhaps typical-of - the condensed sta te of chromatin, and (ii) what is the specific form of arrangement of transcriptionally a ctive chromatin?},
  language  = {en}
}
@article{RunggerCrippaTrendelenburgetal.1978,
  author    = {Rungger, M. and Crippa, M. and Trendelenburg, M. F. and Scheer, Ulrich and Franke, Werner W.},
  title     = {Visualization of rDNA spacer transcription in Xenopus oocytes treated with fluorouridine},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33082},
  year      = {1978},
  abstract  = {Under the intluence of 5-tluoro-uridine, the ultrastructure of the rDNA transcription units in Xenopus oocytes is altered. Whereas part of the matrix units maintains anormal aspect or shows various degrees of inhibition, in a strong proportion of the transcription units the alternating pattern of matrix units and fibril-free spacer regions is no longer recognized. Transcriptional complexes are found along the entire DNP axis, including the regions of the spacers. These observations support biochemical data on transcription in rDNA spacer region.},
  language  = {en}
}
@article{KrohneFrankeScheer1978,
  author    = {Krohne, Georg and Franke, Werner W. and Scheer, Ulrich},
  title     = {The major polypeptides of the nuclear pore complex},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-33078},
  year      = {1978},
  abstract  = {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.},
  language  = {en}
}
@inproceedings{FrankeScheerTrendelenburgetal.1978,
  author    = {Franke, Werner W. and Scheer, Ulrich and Trendelenburg, Michael F. and Zentgraf, H. and Spring, H.},
  title     = {Morphology of transcriptionally active chromatin},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-41097},
  year      = {1978},
  abstract  = {Some decades ago it was noted by cytologists that within the interphase nucleus large portions of the transcriptionally ("genetically," in their terms) inactive chromosomal material are contained in aggregates of condensed chromatin, the "chromocenters," whereas transcriptionally active regions of chromosomes appear in a more dispersed form and are less intensely stained with DNA-directed staining procedures (Heitz 1929, 1932, 1956; Bauer 1933). The hypothesis that condensed chromatin is usually characterized by very low or no transcriptional activity, and that transcription occurs in loosely packed forms of chromatin (including, in most cells, the nucleolar chromatin) has received support from studies of ultrathin sections in the electron microscope and from the numerous attempts to separate transcriptionally active from inactive chromatin biochemically (for references, see Anderson et al. 1975; Berkowitz and Doty 1975; Krieg and Wells 1976; Rickwood and Birnie 1976; Gottesfeld 1977). Electron microscopic autoradiography has revealed that sites of RNA synthesis are enriched in dispersed chromatin regions located at the margins of condensed chromatin (Fakan and Bernhard 1971, 1973; Bouteille et al. 1974; Bachellerie et al. 1975) and are characterized by the occurrence of distinct granular and fibrillar ribonucleoprotein (RNP) structures, such as perichromatin granules and fibrils. The discovery that, in most eukaryotic nuclei, major parts of the chromatin are organized in the form of nucleosomes (Olins and Olins 1974; Kornberg 1974; Baldwin et al. 1975) has raised the question whether the same nucleosomal packing of DNA is also present in transcriptionally active chromatin strands. Recent detailed examination of the morphology of active and inactive chromatin involving a diversity of electron microscopic methods, particularly the spreading technique by Miller and coworkers (Miller and Beatty 1969; Miller and Bakken 1972), has indicated that the DNA of some actively transcribed regions is not packed into nucleosomal particles but is present in a rather extended form within a relatively thin (4-7 nm) chromatin fiber.},
  language  = {en}
}