Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A
Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A
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DOI：
10.1074/jbc.m011153200
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发表时间：
2001-05-04
影响因子：
4.8
通讯作者：
Lindsey, G
中科院分区：
文献类型：
--
作者：
Jason, LJM;Moore, SC;Lindsey, G
用定量琼脂糖凝胶电泳法和分析离心法对泛素化的组蛋白H_2A(UH_2A)取代H_2A的12聚体核小体阵列的折叠进行了分析，两种类型的分析都表明uH_2A阵列达到了与对照相似的紧凑度。2 mm氯化镁中的阵列。这些结果表明，在所测试的离子条件下，泛素与H_2A的结合对核小体阵列形成高阶折叠结构的能力几乎没有影响，相反，在较低的MgCl2浓度下，uH_2A阵列被发现齐聚，提示组蛋白泛素化可能在核小体纤维结合中起作用。
The MgCl2-induced folding of defined 12-mer nucleosomal arrays, in which ubiquitinated histone H2A (uH2A) replaced H2A, was analyzed by quantitative agarose gel electrophoresis and analytical centrifugation, Both types of analysis showed that uH2A arrays attained a degree of compaction similar to that of control. arrays in 2 mM MgCl2. These results indicate that attachment of ubiquitin to H2A has little effect on the ability of nucleosomal arrays to form higher order folded structures in the ionic conditions tested, In contrast, uH2A arrays were found to oligomerize at lower MgCl2 concentrations than control nucleosomal arrays, suggesting that histone ubiquitination may play a role in nucleosomal fiber association.