@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{BenaventeSchmidtZachmannHuegleDoerretal.1988,
  author    = {Benavente, Ricardo and Schmidt-Zachmann, Marion S. and H{\"u}gle-D{\"o}rr, B. and Reimer, G. and Rose, K. M. and Scheer, Ulrich},
  title     = {Identification and definition of nucleolus-related fibrillar bodies in micronucleated cells},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-39423},
  year      = {1988},
  abstract  = {Small nucleolus-related bodies which occur in the nUcleoplasm of " micronuclei" lacking nucleolar organizers have been studied by immunofluorescence microscopy. These bodies stained specifically with three different antibodies directed against proteins that are normally associated with the dense fibrillar component of functional nucleoli, but not with antibodies specific for certain proteins of the granular component or the fibrillar centers. Our data show that, in the absence of rRNA genes, the various constituent proteins characteristic of the dense fibrillar component spontaneously assemble into spherical entities but that the subsequent fusion of these bodies into larger structures is prevented in these micronuclei. The similarity between these nucleolus-related bodies of micronuclei and the prenucleolar bodies characteristic of early stages of nucleologenesis during mitotic telophase is discussed.},
  language  = {en}
}