HISTONE H2B (AND H2A) UBIQUITINATION ALLOWS NORMAL HISTONE OCTAMER AND CORE PARTICLE RECONSTITUTION

被引：32

作者：

DAVIES, N ^{[1
]}

LINDSEY, GG ^{[1
]}

机构：

[1] UNIV CAPE TOWN,DEPT BIOCHEM,RONDEBOSCH 7700,SOUTH AFRICA

来源：

BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION | 1994年 / 1218卷 / 02期

关键词：

UBIQUITIN; HISTONE; CORE PARTICLE; NUCLEOSOME;

D O I：

10.1016/0167-4781(94)90009-4

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：

146 bp core particles were assembled from reconstituted hybrid histone octamers where either histone H2A or H2B were replaced by their ubiquitinated counterparts uH2A and uH2B. No difference in the structure of the core particles was evident upon DNase 1 digestion suggesting that ubiquitination of these histones was not a barrier to normal core particle formation.

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页码：187 / 193

页数：7

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