Sarnow P, Rasched I, Knippers R
Biochim Biophys Acta. 1981 Oct 27;655(3):349-58. doi: 10.1016/0005-2787(81)90045-9.
A histone H4-specific methyltransferase was purified 80-100-fold from nuclei of calf lymphocytes and from calf thymus. Some biochemical properties of the enzyme are described. The enzyme transfers in vitro methyl groups from S-adenosylmethionine preferentially to the lysine residue 20 of histone H4. This is the major in vivo methylation site of H4. DNA-bound or nucleosomal H4 is not methylated in vitro. We have used methylated and unmodified H4 (in the presence of sufficient quantities of the other core histones) for nucleosome reconstitution in vitro and have not found significant differences in the efficiencies of assembly.
从小牛淋巴细胞和小牛胸腺的细胞核中纯化出一种组蛋白H4特异性甲基转移酶,纯化倍数达80至100倍。描述了该酶的一些生化特性。该酶在体外将S-腺苷甲硫氨酸的甲基优先转移至组蛋白H4的赖氨酸残基20。这是H4在体内的主要甲基化位点。结合DNA的或核小体中的H4在体外不被甲基化。我们已使用甲基化和未修饰的H4(在存在足够量其他核心组蛋白的情况下)进行体外核小体重组,且未发现组装效率有显著差异。