H3.H4 TETRAMER DIRECTS DNA AND CORE HISTONE OCTAMER ASSEMBLY IN THE NUCLEOSOME CORE PARTICLE

被引：69

作者：

JORCANO, JL ^{[1
]}

RUIZCARRILLO, A ^{[1
]}

机构：

[1] MAX PLANCK INST MOLEC GENET, D-1000 BERLIN 33, FED REP GER

来源：

BIOCHEMISTRY | 1979年 / 18卷 / 05期

关键词：

D O I：

10.1021/bi00572a005

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 way in which histones interact with DNA during in vitro assembly of nucleohistone has been examined. Chicken erythrocyte core histones H2A, H2B, H3, and H4 and XDNA in 2 M NaCl were allowed to interact by stepwise decrease in the salt concentration. Binding, although weak, was first observed at 1.4 M NaCl and was essentially completed at 0.6 M NaCl. Analysis of the DNA-bound histones revealed that each of the histones in the pairs H2A, H2B and H3, H4 was always present in equimolar amounts and that the relative proportion of each pair was constant between 1.4 and 0.8 M NaCl. Evidence is presented suggesting that binding. © 1979, American Chemical Society. All rights reserved.

引用

页码：768 / 774

页数：7

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