Magnesium-dependent association and folding of oligonucleosomes reconstituted with ubiquitinated H2A

被引：31

作者：

Jason, LJM ^{[1
]}

Moore, SC

Ausió, J

Lindsey, G

机构：

[1] Univ Cape Town, Dept Biochem, ZA-7701 Rondebosch, South Africa

[2] Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 3P6, Canada

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2001年 / 276卷 / 18期

关键词：

D O I：

10.1074/jbc.M011153200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：14597 / 14601

页数：5

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