pH effects on the structure of the inner histones.
The structure of the inner histone complex extracted from chicken erythrocyte chromatin with 2 M NaCl has been studied as a function of pH. At pH 6, the complex dissociates to (H3-H4)2 tetramer and H2A.H2B dimer, with little change in alpha-helix content (as monitored by circular dichroism at 222 mm). Although the circular dichroism of tyrosyl side chains is also largely unchanged by the dissociation, measurements of intrinsic fluorescence do suggest a change in the environment of one or more tyrosines as a result of dissociation. Below pH 4, the histones become partially unfolded, lose specific secondary and tertiary structure, and undergo nonspecific aggregation. Both the pH 6 and 4 transitions, which are largely reversible, parallel pH-induced structural changes of nucleosomes (Zama, M., Olins, D.E., Prescott, B. and Thomas, G.J. (1978) Nucleic Acids Res. 5, 3881-3897). The results are consistent with the presence of tyrosine residues at the histone subunit-subunit contacts and suggest that histone conformation within the globular regions is largely independent of histone-DNA interactions.
D000818:Animals; D002645:Chickens; D002843:Chromatin / Q000378:metabolism; D002942:Circular Dichroism; D004912:Erythrocytes / Q000378:metabolism; D006657:Histones / Q000097:blood; D006863:Hydrogen-Ion Concentration; D011487:Protein Conformation; D013056:Spectrophotometry, Ultraviolet
D002843:Chromatin; D006657:Histones