Conformational effects of organic solvents on histone complexes
Abstract:
Changes in the conformations of H3-H4, H2A-H2B, and the core histone complex brought about by the addition of organic solvents have been examined by circular dichroism spectroscopy. All three complexes assume increased alpha helicity with increasing amounts of the organic solvent. An amount of secondary structure equal to that obtained in phosphate-buffered 2 M NaCl solution can be induced in low-salt solutions of the complexes by the addition of 40-50% ethylene glycol, 50% glycerol, or approximately 2% hexafluoro-2-propanol. H3-H4 was found to be somewhat more flexible than H2A-H2B in its response to changes in solvent polarity. Upon being heated, H3-H4 and the core histone complex both undergo irreversible alpha leads to beta transitions in 50% ethylene glycol under low-salt conditions, while H2A-H2B undergoes an essentially reversible alpha leads to beta random-coil transition under the same conditions. These results are discussed in terms of the dynamics of the nucleosome particle.
Related Concept Videos
Nucleosome Remodeling
Nucleosome remodeling complex
Eukaryotic cells have specialized enzymes called ATP-dependent nucleosome remodeling enzymes. These enzymes...
Histone Modification
Acetylation
The enzyme histone acetyltransferase adds acetyl group to the histones. Another enzyme, histone deacetylase,...
Entropy and Solvation
Solvating Effects
Chemical Shift: Internal References and Solvent Effects
The internal reference compound generally used in NMR spectroscopy is tetramethylsilane (TMS). TMS is preferred because it is chemically inert, soluble in NMR solvents, and easily removable. Also, the highly shielded methyl protons in TMS yield an intense...
The Nucleosome Core Particle
Nucleosomes, paradoxically, perform two opposite functions simultaneously. On the one hand, their primary aim is to protect the delicate DNA strands from physical damage and help achieve a higher compaction ratio. On the other hand, they must allow polymerase enzymes to access histone-bound DNA during...


