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组蛋白乙酰化增加了染色质的溶解度,并在大部分染色质上依次发生。这是一个关于组蛋白乙酰化生物学作用的新模型。

Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation.

作者信息

Perry M, Chalkley R

出版信息

J Biol Chem. 1982 Jul 10;257(13):7336-47.

PMID:7085629
Abstract

The effect of histone acetylation on chromatin solubility has been studied. Nucleosome cores are fairly soluble over a range of Mg2+ and Na+ concentrations. Increasing the amount of Na+ relative to a fixed concentration of Mg2+ leads to increased solubility. Although the effect is not large, acetylated cores are more soluble than control cores, all other factors being equal. Acetylated oligonucleosomes are vastly more soluble than control oligonucleosomes with the greatest differential seen in the presence of Mg2+ at low ionic strengths. Solubility of acetylated oligonucleosomes is favored when the majority of the histones in the nucleosomes are all highly acetylated. Contiguous highly acetylated nucleosomes are enriched in the rapid kinetic form of histone acetylation after short term exposure to butyrate. These observations have been exploited in a fractionation scheme for chromatin based on the levels of hyperacetylation attained after varied times of exposure to sodium butyrate. Essentially all DNA sequences in an unsynchronized cell population are associated with rapidly acetylated histones. Since it is highly unlikely that each cell has its own discrete set of sequences bound to acetylated histone and since the amount of rapidly acetylated histone in a single cell is relatively small (approximately 10% of total histone), we surmise that rapid acetylation migrates throughout much of the chromatin, perhaps in a sequential and highly organized manner. We postulate that the biological role of histone acetylation is to provide a means for sequentially exposing the entire chromatin for surveillance for DNA damage and possibly for recognition of different regions of the DNA by specific (regulatory?) proteins.

摘要

组蛋白乙酰化对染色质溶解性的影响已得到研究。核小体核心在一定范围的Mg2+和Na+浓度下相当易溶。相对于固定浓度的Mg2+增加Na+的量会导致溶解性增加。尽管这种影响不大,但在所有其他因素相同的情况下,乙酰化的核心比对照核心更易溶。乙酰化的寡核小体比对照寡核小体的溶解性要高得多,在低离子强度下存在Mg2+时差异最为显著。当核小体中的大多数组蛋白都高度乙酰化时,乙酰化寡核小体的溶解性更有利。短期暴露于丁酸盐后,连续高度乙酰化的核小体富含组蛋白乙酰化的快速动力学形式。基于暴露于丁酸钠不同时间后达到的高乙酰化水平,这些观察结果已被用于染色质的分级分离方案中。在未同步化的细胞群体中,基本上所有的DNA序列都与快速乙酰化的组蛋白相关。由于每个细胞都有自己一套与乙酰化组蛋白结合的离散序列的可能性极小,而且单个细胞中快速乙酰化组蛋白的量相对较少(约占总组蛋白的10%),我们推测快速乙酰化在大部分染色质中迁移,可能是以一种有序且高度有组织的方式。我们假设组蛋白乙酰化的生物学作用是提供一种手段,用于依次暴露整个染色质以监测DNA损伤,并可能用于特定(调节?)蛋白识别DNA的不同区域。

相似文献

1
Histone acetylation increases the solubility of chromatin and occurs sequentially over most of the chromatin. A novel model for the biological role of histone acetylation.组蛋白乙酰化增加了染色质的溶解度,并在大部分染色质上依次发生。这是一个关于组蛋白乙酰化生物学作用的新模型。
J Biol Chem. 1982 Jul 10;257(13):7336-47.
2
The effect of histone hyperacetylation on the nuclease sensitivity and the solubility of chromatin.组蛋白高度乙酰化对染色质核酸酶敏感性及溶解性的影响。
J Biol Chem. 1981 Apr 10;256(7):3313-8.
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Histone acetylation reduces H1-mediated nucleosome interactions during chromatin assembly.组蛋白乙酰化在染色质组装过程中减少了H1介导的核小体相互作用。
Exp Cell Res. 1991 Oct;196(2):337-45. doi: 10.1016/0014-4827(91)90269-z.
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Influence of histone acetylation on the solubility, H1 content and DNase I sensitivity of newly assembled chromatin.组蛋白乙酰化对新组装染色质的溶解性、H1含量及DNase I敏感性的影响
Nucleic Acids Res. 1989 Jun 12;17(11):4275-91. doi: 10.1093/nar/17.11.4275.
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Effect of histone acetylation on structure and in vitro transcription of chromatin.组蛋白乙酰化对染色质结构及体外转录的影响。
Nucleic Acids Res. 1978 Oct;5(10):3523-47. doi: 10.1093/nar/5.10.3523.
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Factors affecting nucleosome structure in transcriptionally active chromatin. Histone acetylation, nascent RNA and inhibitors of RNA synthesis.影响转录活性染色质中核小体结构的因素。组蛋白乙酰化、新生RNA及RNA合成抑制剂。
Eur J Biochem. 1990 Dec 27;194(3):811-23. doi: 10.1111/j.1432-1033.1990.tb19474.x.
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Analysis of nucleosome assembly and histone exchange using antibodies specific for acetylated H4.使用针对乙酰化H4的特异性抗体分析核小体组装和组蛋白交换。
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Parental nucleosomes segregated to newly replicated chromatin are underacetylated relative to those assembled de novo.与那些重新组装的核小体相比,分离到新复制染色质上的亲代核小体处于低乙酰化状态。
Biochemistry. 1993 Dec 14;32(49):13615-23. doi: 10.1021/bi00212a029.
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Histone acetylation alters the capacity of the H1 histones to condense transcriptionally active/competent chromatin.组蛋白乙酰化改变了H1组蛋白凝聚转录活性/有转录能力的染色质的能力。
J Biol Chem. 1990 Mar 25;265(9):5150-6.
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Acetylation of histone H4 plays a primary role in enhancing transcription factor binding to nucleosomal DNA in vitro.组蛋白H4的乙酰化在体外增强转录因子与核小体DNA的结合中起主要作用。
EMBO J. 1996 May 15;15(10):2508-18.

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