Neutron scattering studies of the H2a-H2b and (H3-H4)2 histone complexes.
Neutron scattering experiments have shown that both the (H3-H4)2 and H2a-H2b histone complexes are quite asymmetric in solution. The (H3-H4)2 tetramer is an oblate or flattened structure, with a radius of gyration almost as large as that of the core octamer. If the tetramer is primarily globular, it must have an axial ratio of about 1:5. It is more likely, however, that this asymmetry results in part from N-terminal arms that extend outward approximately within the major plane of the particle. If this is the case, less asymmetric models for the globular part of the tetramer, including a dislocated disk of the type proposed by Klug et al. (23), can be made consistent with the scattering data. The H2a-H2b dimer, on the other hand, is an elongated structure. The low resolution data are in good agreement with those calculated for a cylindrical model 64 X 27 A, but other elongated models fit those data almost as well, including one that approximates free N-terminal arms at each end. Free arms are not necessary, but they must extend from the ends if they exist. A contrast matching experiment done with 50% deuterated H2b and undeuterated H2a in the reconstituted dimer showed that these two histones must each be rather elongated within the complex and are not just confined to one end. The amount of scattering contrast between the undeuterated and 50% deuterated histones was sufficient to suggest further experiments using complexes reconstituted from mixtures of undeuterated and partially deuterated histones which will help elucidate their arrangement within the histone complexes and within the octamer core of the nucleosome core particle.
D000818:Animals; D002467:Cell Nucleus / Q000648:ultrastructure; D002645:Chickens; D002843:Chromatin / Q000648:ultrastructure; D003903:Deuterium; D004912:Erythrocytes / Q000648:ultrastructure; D005055:Euglena; D006657:Histones / Q000097:blood / Q000302:isolation & purification; D046911:Macromolecular Substances; D008958:Models, Molecular; D009502:Neutrons; D011487:Protein Conformation; D012542:Scattering, Radiation
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances; D003903:Deuterium