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Exchange of proteins during immunofractionation of chromatin.

作者信息

Landsman D, Mendelson E, Druckmann S, Bustin M

出版信息

Exp Cell Res. 1986 Mar;163(1):95-102. doi: 10.1016/0014-4827(86)90561-6.

DOI:10.1016/0014-4827(86)90561-6
PMID:3510889
Abstract

The migration and rearrangement of chromosomal proteins during immunofractionation of chromatin has been investigated. Oligonucleosomes from two different chromatins, chicken erythrocyte or rat liver, were mixed with oligonucleosomes from the other species which had been depleted of histones H1/H5 and high mobility group proteins (HMGs). The mixture was treated with buffers of various ionic strengths and immunofractionated on an anti-H1 degrees/H5 or anti-HMG-17 IgG-Sepharose column. The type of DNA, which was retained as the bound fraction on the column, was determined by slot blot analysis using nick-translated repetitive DNA probes from either chicken or rat. The results indicate that in low ionic strength buffers (i.e., below 40 mM NaCl), there is very little exchange of either histone H5 or HMG-17 among nucleosomes and therefore we suggest that it is possible to fractionate nucleosomes according to their antigenic content.

摘要

相似文献

1
Exchange of proteins during immunofractionation of chromatin.
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2
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HMGN proteins act in opposition to ATP-dependent chromatin remodeling factors to restrict nucleosome mobility.HMGN蛋白的作用与ATP依赖的染色质重塑因子相反,以限制核小体的移动性。
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Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins.高迁移率族染色体蛋白的功能基序对DNA依赖性活动的调控
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Deposition of chromosomal protein HMG-17 during replication affects the nucleosomal ladder and transcriptional potential of nascent chromatin.复制过程中染色体蛋白HMG-17的沉积会影响新生染色质的核小体梯状结构和转录潜能。
EMBO J. 1993 Oct;12(10):3855-64. doi: 10.1002/j.1460-2075.1993.tb06064.x.
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The cooperative binding of chromosomal protein HMG-14 to nucleosome cores is reduced by single point mutations in the nucleosomal binding domain.核小体结合结构域中的单点突变会降低染色体蛋白HMG - 14与核小体核心的协同结合。
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6
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