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  • 1
    Electronic Resource
    Electronic Resource
    Studies on chromatin (1975)
    Springer
    Molecular biology reports 2 (1975), S. 247-254 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Electron microscopy of purified chromatin subunits (ν-bodies [17] or nucleosomes [2] revealed a hole or at least a deep indentation in the globular nucleosome. A hole in the nucleosome was visualized using rotatory shadowing with platinum-palladium or more directly, by negative staining with sodium phosphotungstate. The diameter of the hole as measured from negatively stained samples is 10–25Å. The external diameter of the negatively stained nucleosome equals 75±15Å. Although most of the data are formally compatible with either a hole or a deep indentation in the nucleosome, some views of the particles in the negatively stained samples suggest a hole rather than an indentation. The possible significance of a toroidal structure of the chromatin subunit is discussed in the accompanying paper [3].
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00356995
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Separation of nucleosomes containing histones H1 and H5 (1978)
    Springer
    Molecular biology reports 4 (1978), S. 185-189 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Hen erythrocyte chromatin was digested with staphylococcal nuclease and fractionated by electrophoresis in polyacrylamide gels. Instead of the three bands described for mouse carcinoma chromatin, four main discrete components (MN1, MN2, MN2E and MN3) were resolved in the mononucleosome fraction of erythrocyte chromatin. MN2 contained all five histones and a DNA fragment of 165–180 base pairs. MN2E comprised four nucleosomal histones plus histone H5 (but not H1) and a DNA fragment of 170–190 base pairs. The relatively nuclease resistant MN3 fraction of erythrocyte nucleosomes contained H1 but no H5 histone. A more accurate analysis of the MN2 fraction in mouse carcinoma nucleosomes revealed some additional microheterogeneity depending on the presence of two different subfractions of H1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00777522
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Studies on protein organization of nucleosomes using cross-linking (1981)
    Springer
    Molecular biology reports 7 (1981), S. 209-216 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract When chromosomal proteins in chromatin or in mononucleosomes were extensively cross-linked with an imido ester, the H1-containing nonameric histone complex was revealed. In this complex, histone H1 is connected with the octamer of core histones. The cross-linking of H1 to the octamer is realized preferentially through H2a and H3 histones. Some HMG (high mobility group) proteins located presumably in the linker regions of a nucleosome fiber also take part in the formation of dimers, possibly with the histones of a nucleosomal core. The results suggest mutual interactions between some linker-associated proteins and intranucleosomal histones. Experiments involving extensive cross-linking of proteins in the purified mononucleosome subfractions demonstrated differences in the organization of core histones between ‘complete’ nucleosomes and nucleosomes lacking H1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00805754
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Studies on chromatin (1975)
    Springer
    Molecular biology reports 2 (1975), S. 209-217 
    Details
    ISSN: 1573-4978
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Chromatin lacking histone H1 was found by electron microscopy to contain ‘beaded’ deoxyribonucleoprotein fibers. Adjacent beads are connected with each other by threads having a DNA-like appearance. At least some of threads are shown to be free DNA stretches. Average length and the content of free DNA stretches in histone H1-depleted chromatin depends on the ionic conditions of the medium. The appearance of individual beads is similar to that of chromatin subunits or v-bodies [1] in the original chromatin. Thus, in agreement with the X-ray data [2], histone H1 apparently is not required for maintenance of a compact state of DNA in chromatin subunits.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00356990
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    Paper (German National Licenses)
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  • 5
    Electronic Resource
    Electronic Resource
    Studies on structure and function of chromatin (1981)
    Springer
    Molecular and cellular biochemistry 40 (1981), S. 29-48 
    Details
    ISSN: 1573-4919
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Notes: Summary This article covers research work in this laboratory on the structure and function of chromatin. Early studies have led to discovery of skeletal fibrills (nucleonemas) within the nuclei and showed the specific role of histone H1 in chromatin condensation and in restriction of transcription. More recently with the aid of a novel DNP electrophoresis technique the relation of histone HI and non-histone proteins to nucleosomes was studied. Three types of mononucleosomes and a number of subnucleosomes were identified in chromatin digests. The complexes of certain HMG proteins with short DNA segments were isolated and found to originate from transcriptionally active chromatin. Different forms of SV40 minichromosome were characterized. A method for the analysis of nucleosome distribution along the DNA sequence was elaborated and used to show non-random (phased) location of nucleosomes on SV40 DNA. The attachment of DNA to skeletal elements of interphase nuclei and metaphase chromosomes was shown to be a non-random, probably sequence-specific process.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00230186
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    Paper (German National Licenses)
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