Crystallographic Structure of the Octameric Histone Core of the Nucleosome at a Resolution of 3.3 Å

Abstract

The structure of the (H2A-H2B-H3-H4)2 histone octamer has been determined by means of x-ray crystallographic techniques at a resolution of 3.3 angstroms. The octamer is a prolate ellipsoid 110 angstroms long and 65 to 70 angstroms in diameter, and its general shape is that of a rugby ball. The size and shape are radically different from those determined in earlier studies. The most striking feature of the histone octamer is its tripartite organization, that is, a central (H3-H4)2 tetramer flanked by two H2A-H2B dimers. The DNA helix, placed around the octamer in a path suggested by the features on the surface of the protein, appears like a spring holding the H2A-H2B dimers at either end of the (H3-H4)2 tetramer.

Dynamics of interaction of RNA polymerase II with nucleosomes. I. Effect of salts

“…In the presence of 0.2 M AcOK, binding of pol I1 to nucleosomes resulted in changes in the excited state solvent interactions in the TRES and a blue shift of the steady state as well as the 502-nm TRES peak, all suggesting a more hydrophobic surrounding for the dye. In addition, the lack of mobility of solvent molecules in the probe's surroundings indicated blocking of the open solvent channels of the nucleosomes (Burlingame et al, 1985;Arents et al, 1991), which were probably available in all other cases. Figure 6 is an attempt to collectively describe all the conformational changes of nucleosomes found in this study through a diagrammatic representation of the histone octamer in the nucleosome (based on the structure given originally by Burlingame et al [1985]).…”

“…In addition, the lack of mobility of solvent molecules in the probe's surroundings indicated blocking of the open solvent channels of the nucleosomes (Burlingame et al, 1985;Arents et al, 1991), which were probably available in all other cases. Figure 6 is an attempt to collectively describe all the conformational changes of nucleosomes found in this study through a diagrammatic representation of the histone octamer in the nucleosome (based on the structure given originally by Burlingame et al [1985]). Although these authors have revised their structure, the description of the solvent channels, which forms the basis of the model given in Figure 6, remains unchanged (Arents et al, 1991).…”

Structural aspects of protein-DNA recognition

“…However, there are subtle differences in the mode of DNA recognition and interaction displayed by these repressors, the details of which will be discussed later. On the other hand, the three helix-turn-helix repressors listed in Table 1 Beese & Steitz (1991 Beese & Steitz (1991) Freemont et al (1988) Steitz (1990) White et al (1989) Sanderson et al (1990 Burlingame et al (1985) Richmond et al (1984 is involved in the regulation of tryptophan biosynthesis by binding as a dimer to three different operator sites in the presence of its corepressor L-tryptophan (Klig et al, 1988). Binding in the absence of L-tryptophan is weak and non-specific.…”

The reconstitution of a hybrid histone octamer containing avian 110Cys‐des‐thio‐histone H3 and sea‐urchin 73Cys‐histone H4

“…The highest level of insight, however, has not yet been reached. This has primarily been due to the limited resolution attained during studies of the core particle [l] and the different ultrastructural descriptions of the core particle yielded from the studies of Richmond et al [l] and Burlingame et al [2].…”

“…The highest level of insight, however, has not yet been reached. This has primarily been due to the limited resolution attained during studies of the core particle [l] and the different ultrastructural descriptions of the core particle yielded from the studies of Richmond et al [l] and Burlingame et al [2].The reconstitution and physicochemical characterisation of histone octamers carrying reporter molecules in well-defined positions represent an alternative approach to the study of histone-histone and histone-DNA interactions. Such studies, undertaken in parallel with crystallographic investigations at the present and improved resolution, will increase the level of insight into the underlying mechanisms of biologically significant structural changes in the core particle.…”