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染色质核心颗粒低盐转变的可逆性。

Reversibility of the low-salt transition of chromatin core particles.

作者信息

Libertini L J, Small E W

出版信息

Nucleic Acids Res. 1987 Aug 25;15(16):6655-64. doi: 10.1093/nar/15.16.6655.

DOI:10.1093/nar/15.16.6655
PMID:3628003
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC306129/
Abstract

The low-salt transition of chromatin core particles is reversible if the monovalent cation concentration is kept above 0.2 mM. Exposure of the particles to salt concentrations below this value results in a nonreversible secondary transition. The nonreversible changes are relatively slow with a half-time of about 15 minutes. Once exposed to such low ionic strength, the particles then begin to refold with increasing salt in at least two steps over a much higher ionic strength range than is required for the usual low-salt transition. The refolding is very fast, with a half-time less than a minute. Small differences between particles which had or had not been exposed to very low salt persist even when the particles are returned to near physiological ionic strengths.

摘要

如果单价阳离子浓度保持在0.2 mM以上,染色质核心颗粒的低盐转变是可逆的。将颗粒暴露于低于该值的盐浓度会导致不可逆的二级转变。不可逆变化相对较慢,半衰期约为15分钟。一旦暴露于如此低的离子强度,颗粒随后开始在比通常低盐转变所需的离子强度范围高得多的范围内,至少分两步随着盐浓度增加而重新折叠。重新折叠非常快,半衰期不到一分钟。即使颗粒恢复到接近生理离子强度,暴露于极低盐浓度和未暴露于极低盐浓度的颗粒之间的微小差异仍然存在。

相似文献

1
Reversibility of the low-salt transition of chromatin core particles.染色质核心颗粒低盐转变的可逆性。
Nucleic Acids Res. 1987 Aug 25;15(16):6655-64. doi: 10.1093/nar/15.16.6655.
2
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Histone hyperacetylation. Its effects on nucleosome core particle transitions.组蛋白高度乙酰化。其对核小体核心颗粒转变的影响。
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本文引用的文献

1
Iodination of nucleosomes at low ionic strength: conformational changes in H4 and stabilization by H1.低离子强度下核小体的碘化作用:H4的构象变化及H1的稳定作用
Nucleic Acids Res. 1981 Sep 11;9(17):4367-85. doi: 10.1093/nar/9.17.4367.
2
Structural conformations of nucleosomes at low ionic strength from flow birefringence and intrinsic viscosity.通过流动双折射和特性粘度研究低离子强度下核小体的结构构象。
Biopolymers. 1981 Apr;20(4):719-52. doi: 10.1002/bip.1981.360200408.
3
Effects of pH on low-salt transition of chromatin core particles.pH对染色质核心颗粒低盐转变的影响。
Biochemistry. 1982 Jul 6;21(14):3327-34. doi: 10.1021/bi00257a013.
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Optical model studies of salt-induced conformational transitions in the nucleosome.核小体中盐诱导构象转变的光学模型研究。
Biochemistry. 1982 Mar 16;21(6):1177-86. doi: 10.1021/bi00535a011.
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Unfolding of 175-base-pair nucleosomes.175个碱基对核小体的解折叠
Biochemistry. 1982 Feb 16;21(4):664-9. doi: 10.1021/bi00533a012.
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Nucleosome structure.核小体结构。
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Proc Natl Acad Sci U S A. 1981 Nov;78(11):6803-7. doi: 10.1073/pnas.78.11.6803.
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Effect of DNA length on the nucleosome low salt transition.DNA长度对核小体低盐转变的影响。
Nucleic Acids Res. 1980 Jun 11;8(11):2475-87. doi: 10.1093/nar/8.11.2475.
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Structural changes of nucleosomes in low-salt concentrations.低盐浓度下核小体的结构变化。
Biochemistry. 1979 Sep 4;18(18):3960-5. doi: 10.1021/bi00585a018.
10
Specific histone-histone contacts are ruptured when nucleosomes unfold at low ionic strength.当核小体在低离子强度下展开时,特定的组蛋白-组蛋白接触会破裂。
Biochemistry. 1979 Mar 20;18(6):1082-9. doi: 10.1021/bi00573a023.