The structure of the histone dimer H2A-H2B studied by spectroscopy.
The spatial organization of the histone dimer (H2A-H2B) in 0.1-1.0 M NaCl is characterized by the inclusion of 38% of the residues in alpha-helical segments, an average fluorescence quantum yield of 0.085 +/- 0.003, a red shift of absorption (lambda max = 278 +/- 0.5 nm) and fluorescent spectra (lambda max = 304.4 +/- 0.3 nm) as compared to the respective spectra of free tyrosine. The changing of position lambda max of tyrosine fluorescence of histones during denaturation has been shown. The dimer (H2A-H2B) exhibited a conformational change in a transition centred at about 0.5 M NaCl. The dimer denaturation takes place at higher urea concentrations as the ionic strength of the medium increases. The quenching of tyrosine fluorescence of the histone dimer (H2A-H2B) was performed using the ions I-, Cs+ and acrylamide. It has been shown that, at a concentration of NaCl over 0.5 M, dimer compactization takes place, as well as the screening of some part of tyrosyls for te against the quenching effect of Cs+. Our experiments made it possible to identify three zones in the composition of the histone dimer (H2A-H2B) and determine the number (ni) and fluorescence quantum yields (qi) of tyrosyls included in the following specific zones: zone I, n1 = 2, q1 = 0.136; zone II, n2 = 3; q2 = 0.08; zone III, n3 = 3; q3 = 0.055.
D000818:Animals; D002417:Cattle; D002458:Cell Fractionation; D002467:Cell Nucleus / Q000648:ultrastructure; D002843:Chromatin / Q000648:ultrastructure; D002850:Chromatography, Gel; D002942:Circular Dichroism; D006657:Histones / Q000302:isolation & purification*; D046911:Macromolecular Substances; D008970:Molecular Weight; D011487:Protein Conformation; D013050:Spectrometry, Fluorescence; D013950:Thymus Gland / Q000648:ultrastructure
D002843:Chromatin; D006657:Histones; D046911:Macromolecular Substances