组蛋白h4特异性甲基转移酶

Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis Pub Date : 1981-10-27 DOI:10.1016/0005-2787(81)90045-9

Peter Sarnow , Ihab Rasched, Rolf Knippers

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引用次数: 23

摘要

从小牛淋巴细胞和小牛胸腺细胞核中纯化了一种组蛋白h4特异性甲基转移酶80 - 100倍。介绍了该酶的一些生化特性。该酶在体外将s -腺苷蛋氨酸的甲基优先转移到组蛋白H4的赖氨酸残基20上。这是体内H4的主要甲基化位点。dna结合或核小体H4在体外不甲基化。我们使用甲基化和未修饰的H4(在存在足够数量的其他核心组蛋白的情况下)进行体外核小体重组，并没有发现组装效率的显着差异。

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A histone H4-specific methyltransferase

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.

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Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis

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