The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays
The H4 Tail Domain Participates in Intra- and Internucleosome Interactions with Protein and DNA during Folding and Oligomerization of Nucleosome Arrays
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DOI：
10.1128/mcb.01343-08
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发表时间：
2009-01-15
影响因子：
5.3
通讯作者：
Hayes, Jeffrey J.
中科院分区：
文献类型：
--
作者：
Kan, Pu-Yeh;Caterino, Tamara L.;Hayes, Jeffrey J.
核小体阵列凝聚成更高阶的二级和三级染色质结构可能涉及核小体之间由核心组蛋白尾部结构域介导的长距离相互作用。我们已经表征了由H4尾部结构域介导的阵列间相互作用，已知H4尾部结构域在此类结构的形成中起主导作用。我们发现，在寡核小体阵列的自结合过程中，H4尾部的N端介导了与DNA的阵列间接触，这与之前对H3尾部结构域的发现类似。然而，H4的组蛋白折叠结构域附近的一个位点参与了一系列不同的相互作用，以浓缩结构接触DNA和H2A。此外，我们还发现H4-H2A相互作用通过核小体内和核小体间的方式发生，支持尾部的额外的核小体内功能。有趣的是，H4尾部的乙酰化本身对阵列间相互作用几乎没有影响，但盖过了连接物组蛋白诱导的阵列间相互作用的强烈刺激。我们的结果表明，H4尾部通过一系列与H3尾部结构域不同的潜在排他性相互作用，促进了二级和三级染色质结构的形成。
The condensation of nucleosome arrays into higher-order secondary and tertiary chromatin structures likely involves long-range internucleosomal interactions mediated by the core histone tail domains. We have characterized interarray interactions mediated by the H4 tail domain, known to play a predominant role in the formation of such structures. We find that the N-terminal end of the H4 tail mediates interarray contacts with DNA during self-association of oligonucleosome arrays similar to that found previously for the H3 tail domain. However, a site near the histone fold domain of H4 participates in a distinct set of interactions, contacting both DNA and H2A in condensed structures. Moreover, we also find that H4-H2A interactions occur via an intra- as well as an internucleosomal fashion, supporting an additional intranucleosomal function for the tail. Interestingly, acetylation of the H4 tail has little effect on interarray interactions by itself but overrides the strong stimulation of interarray interactions induced by linker histones. Our results indicate that the H4 tail facilitates secondary and tertiary chromatin structure formation via a complex array of potentially exclusive interactions that are distinct from those of the H3 tail domain.