A nucleosome-like structure containing DNA and the arginine-rich histones H3 and H4.
The low-angle X-ray diffraction pattern from fibres of reconstituted H3/H4/DNA complexes is very similar to that of chromatin and has well defined maxima at 10.6, 5.4, 3.4 and 2.6 nm. Staphyloccal nuclease digestion of reconstituted H3/H4/DNA yields DNA fragments of length 49, 69, 100, 128, 193 and 255 b.p. as principal components. Comparison of the relative amounts of DNA fragments shows that the larger components (100 and 128 b.p.) increase with respect to the smaller (49 and 69 b.p.) as the histone to DNA ratio increases. A structural unit containing intergral of 65 b.p. of DNA and tetrameric (H3/H4)2 is proposed such that longer DNA fragments result from multiples of this unit. The principal nucleo-protein particle resulting from nuclease digestion contains 128/139 b.p. of DNA and has electrophoretic mobility very close to that of 'core' nucleosome. It probably represents a dimer of the basic structural unit.
D000818:Animals; D001120:Arginine; D002417:Cattle; D002467:Cell Nucleus / Q000648:ultrastructure*; D002843:Chromatin; D004247:DNA; D006657:Histones; D008836:Micrococcal Nuclease; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D013950:Thymus Gland; D014961:X-Ray Diffraction
D002843:Chromatin; D006657:Histones; D004247:DNA; D001120:Arginine; D008836:Micrococcal Nuclease