Nicola N A, Fulmer A W, Schwartz A M, Fasman G D
Biochemistry. 1978 May 2;17(9):1779-85. doi: 10.1021/bi00602a032.
Low molecular weight histone complexes of H2A (congruent to dimer), H2B (congruent to tetramer), H3--H4 (congruent to tetramer), H2A--H2B (congruent to dimer), and H2B--H4 (congruent to dimer) have been prepared in 2 M NaCl and neutral pH at 4 degrees C. These materials are free of nonspecific aggregate and are suitable for study by high resolution proton magnetic resonance spectroscopy. Such spectra have been recorded in aqueous solutions under conditions allowing a study of the exchangeable proton resonances of histone complexes for the first time and indicate that the structured regions are rich in hydrophobic amino acids, as well as arginine and some acidic amino acids. Most of the lysine and probably alanine residues remain in a motile, random coil-like state after formation of the complexes. It is suggested that arginine residues may be important in inter- and/or intra-subunit interactions in histone complexes.
已在2M氯化钠和4℃中性pH条件下制备了H2A(相当于二聚体)、H2B(相当于四聚体)、H3 - H4(相当于四聚体)、H2A - H2B(相当于二聚体)和H2B - H4(相当于二聚体)的低分子量组蛋白复合物。这些材料不含非特异性聚集体,适用于高分辨率质子磁共振光谱研究。此类光谱是在水溶液中记录的,首次在允许研究组蛋白复合物可交换质子共振的条件下进行,结果表明结构区域富含疏水氨基酸以及精氨酸和一些酸性氨基酸。大多数赖氨酸残基以及可能的丙氨酸残基在复合物形成后仍处于动态、随机卷曲状状态。有人提出,精氨酸残基可能在组蛋白复合物的亚基间和/或亚基内相互作用中起重要作用。