A model for chromatin based upon two symmetrically paired half-nucleosomes
We propose that the basic unit of chromatin is constructed of two isologously paired heterotypic protein tetramers each containing one molecule of H2A, H2B, H3, and H4 histone. These proteins form a core that holds 140 base pairs (bp) of DNA in a single left-handed, non-interwound DNA super-coil approximately 95 bp in circumference, creating a nucleosome particle (DNA and protein) organized about a dyad axis of symmetry. Such a nucleosome can open up into its separate half-nucleosomes to allow genetic readout without requiring histone displacement.
Electrophoretic comparisons of liver chromatin proteins isolated from heterotic rats during postweaning development
Dependence of mammalian DNA replication on DNA supercoiling. I. Effects of ethidium bromide on DNA synthesis in permeable Chinese hamster ovary cells
Benzo(a)pyrene 7,8-dihydrodiol-9,10-oxide modification of DNA: relation to chromatin structure and reconstitution
Interactions of the histone octamer with single-stranded DNA. Sedimentation analysis and low-angle X-ray diffraction
Hemoglobin switching in sheep: only the gamma gene is in the active conformation in fetal liver but all the beta and gamma genes are in the active conformation in bone marrow
Altered nucleosome structure containing DNA sequences complementary to 19S and 26S ribosomal RNA in Physarum polycephalum
Asymmetric lateral distribution of unshielded phosphate groups in nucleosomal DNA and its role in DNA bending
Histone octamer dissociation is not required for transcript elongation through arrays of nucleosome cores by phage T7 RNA polymerase in vitro
The effect of preincubation of HeLa cell nuclei with ATP on the degradation of mononucleosomal DNA by micrococcal nuclease
Protein kinase in HeLA nucleosomes: a reevaluation of the interactions of histomes with the ends of core particle DNA
Stability of the primary organization of nucleosome core particles upon some conformational transitions
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