ATP DEPENDENT HISTONE PHOSPHORYLATION AND NUCLEOSOME ASSEMBLY IN A HUMAN CELL-FREE-EXTRACT
ATP DEPENDENT HISTONE PHOSPHORYLATION AND NUCLEOSOME ASSEMBLY IN A HUMAN CELL-FREE-EXTRACT
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DOI：
10.1093/nar/19.21.5999
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发表时间：
1991-11-11
影响因子：
14.9
通讯作者：
ALLEN, TD
中科院分区：
文献类型：
--
作者：
BANERJEE, S;BENNION, GR;ALLEN, TD
HeLa细胞提取物中生理间隔的核小体的形成依赖于ATP。在线形和共价闭合的环状DNA上，染色质组装都需要ATP水解酶。我们研究了组蛋白的磷酸化状态和核小体形成之间的联系，我们证明，在没有组蛋白磷酸化的情况下，不会形成稳定的、间隔规则的核小体。磷酸化的H3稳定核小体的核心，而组蛋白H2A的磷酸化是将核小体之间的连接子长度从0增加到大约45bp所必需的。在没有核心组蛋白磷酸化的情况下，单独的组蛋白H1，无论是磷酸化的还是非磷酸化的，都不会增加核小体重复长度。H1和H3的磷酸化与染色质的缩合有关。将核小体的周期从大约150个碱基增加到大约185个碱基所必需的最大ATP水解量，不仅抑制了H1和H3的磷酸化，而且促进了它们的去磷酸化。
Physiologically spaced nucleosome formation in HeLa cell extracts is ATP dependent. ATP hydrolysis is required for chromatin assembly on both linear and covalently closed circular DNA. The link between the phosphorylation state of histones and nucleosome formation has been examined and we demonstrate that in the absence of histone phosphorylation no stable and regularly spaced nucleosomes are formed. Phosphorylated H3 stabilizes the nucleosome core; while phosphorylation of histone H2a is necessary to increase the linker length between nucleosomes from 0 to approximately 45 bp. Histone H1 alone, whether phosphorylated or unphosphorylated, does not increase the nucleosome repeat length in the absence of core histone phosphorylation. Phosphorylations of H1 and H3 correlate with condensation of chromatin. Maximum ATP hydrolysis which is necessary to increase the periodicity of nucleosomes from approximately 150 to approximately 185 bp, not only inhibits H1 and H3 phosphorylation but facilitates their dephosphorylation.