Diez-Caballero T, Avilés F X, Albert A
Nucleic Acids Res. 1981 Mar 25;9(6):1383-93. doi: 10.1093/nar/9.6.1383.
The interaction of calf thymus histone H1 with homologous and heterologous DNA has been studied at different ionic strengths. It has been found that about 0.5 M NaCl histone H1, and its fragments N-H1 (residues 1-72) and C-H1 (residues 73-C terminal), precipitate selectively a small fraction of calf thymus DNA. This selective precipitation is preserved up to very high values (less than 2.0) of the input histone H1/DNA ratio. The percentage of DNA insolubilized by histone H1 under these ionic conditions is dependent upon the molecular weight of the nucleic acid, diminishing from 18% fro a Mw equals 1.0 x 10(7) daltons to 5% for a Mw equals 8.0 x 10(4) daltons. The base composition of the precipitated DNA is similar to that of the bulk DNA. Calf thymus histone H1 also selectively precipitates a fraction of DNA from other eukaryotes (herring, trout), but not from some prokaryotes (E. coli, phage gamma. On the other hand, at 0.5 M NaCl, the whole calf thymus DNA (but not E. coli DNA) presents a limited number of binding sites for histone H1, the saturation ratio histone H1 bound/total DNA being similar to that found in chromatin. A similar behavior is observed from the histone H1 fragments, N-H1 and C-H1, which bind to DNA in complementary saturation ratios. It is suggested that in eukaryotic organisms histone H1 molecules maintain specific interactions with certain DNA sequences. A fraction of such specific complexes could act as nucleation points for the high-order levels of chromatin organization.
已在不同离子强度下研究了小牛胸腺组蛋白H1与同源及异源DNA的相互作用。研究发现,在约0.5M NaCl条件下,组蛋白H1及其片段N-H1(第1-72位氨基酸残基)和C-H1(第73位氨基酸残基至C末端)能选择性沉淀一小部分小牛胸腺DNA。这种选择性沉淀在非常高的输入组蛋白H1/DNA比例值(小于2.0)下仍能保持。在这些离子条件下,被组蛋白H1不溶性沉淀的DNA百分比取决于核酸的分子量,从分子量为1.0×10⁷道尔顿时的18%降至分子量为8.0×10⁴道尔顿时的5%。沉淀DNA的碱基组成与总体DNA相似。小牛胸腺组蛋白H1也能选择性沉淀来自其他真核生物(鲱鱼、鳟鱼)的一部分DNA,但不能沉淀来自某些原核生物(大肠杆菌、噬菌体γ)的DNA。另一方面,在0.5M NaCl条件下,整个小牛胸腺DNA(但不是大肠杆菌DNA)对组蛋白H1有有限数量的结合位点,结合的组蛋白H1/总DNA的饱和比例与染色质中的相似。从组蛋白H1片段N-H1和C-H1也观察到类似行为,它们以互补的饱和比例与DNA结合。有人提出,在真核生物中,组蛋白H1分子与某些DNA序列保持特定相互作用。这类特定复合物的一部分可能作为染色质高级结构组织的成核点。