Histone acetylation alters the capacity of the H1 histones to condense transcriptionally active/competent chromatin.
Histone acetylation alters the capacity of the H1 histones to condense transcriptionally active/competent chromatin.
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组蛋白乙酰化改变 H1 组蛋白压缩转录活性/活性染色质的能力。
DOI：
10.1016/s0021-9258(19)34098-0
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发表时间：
1990
期刊：
影响因子：
--
通讯作者：
J. Davie
中科院分区：
文献类型：
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作者：
J. Ridsdale;Michael J Hendzel;G. Delcuve;J. Davie
研究了组蛋白乙酰化与H1组蛋白引起0.15M氯化钠诱导的转录活性/活性基因染色质片段聚集/沉淀的关系。以前的研究表明，从鸡红细胞中分离到的具有转录活性/活性但不受抑制的染色质多核小体，在与H1组蛋白重组后，在0.15M的氯化钠中仍然是可溶的。这一结果表明，活性/活性基因核小体的某些成分改变了H1组蛋白凝聚染色质纤维的能力。最近，Hebbes et al.(Hebbes，T.R.，Thorne，A.W.和Crane-Robinson，C.(1988)EMBO J.7,1395-1402)直接证明了鸡红系细胞的活跃但未被抑制的基因染色质含有高水平的乙酰化组蛋白。在这里，我们证明了活性/活性基因染色质片段在0.15M氯化钠中的溶解度取决于乙酰化组蛋白种类的水平，超乙酰化的诱导增加了该基因染色质的溶解度。此外，我们还表明，降低乙酰化组蛋白形式的水平降低了活性/活性基因染色质片段抵抗外源添加H1-组蛋白诱导的0.15M氯化钠聚集/沉淀的能力。这些结果表明，组蛋白乙酰化改变了H1组蛋白形成致密的高阶染色质结构的能力，从而使活性/活性基因染色质保持在较少折叠的状态。
The relationship between histone acetylation and the capacity of H1 histones to cause the 0.15 M NaCl-induced aggregation/precipitation of transcriptionally active/competent gene chromatin fragments was investigated. Previous studies have shown that transcriptionally active/competent, but not repressed, gene chromatin polynucleosomes, which were isolated from chicken erythrocytes, remained soluble in 0.15 M NaCl after being reconstituted with H1 histones. This result suggested that some component of the active/competent gene nucleosome altered the capacity of the H1 histones to condense the chromatin fiber. Recently, Hebbes et al. (Hebbes, T.R., Thorne, A.W., and Crane-Robinson, C. (1988) EMBO J. 7, 1395-1402) demonstrated directly that active, but not repressed, gene chromatin of chicken erythroid cells contain high levels of acetylated histones. Here, we show that the solubility of active/competent gene chromatin fragments in 0.15 M NaCl is dependent on the level of acetylated histone species, with induction of hyperacetylation increasing the solubility of this gene chromatin. Also, we show that lowering the levels of the acetylated histone forms reduces the ability of the active/competent gene chromatin fragments to resist exogenously added H1-histone-induced 0.15 M NaCl aggregation/precipitation. These results suggest that histone acetylation alters the capacity of the H1 histones to form compact higher order chromatin structures such that active/competent gene chromatin is maintained in a less folded state than the bulk of chromatin.