Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails
Preferential binding of the histone (H3-H4)2 tetramer by NAP1 is mediated by the amino-terminal histone tails
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DOI：
10.1074/jbc.m305636200
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发表时间：
2003-11-07
影响因子：
4.8
通讯作者：
Luger, K
中科院分区：
文献类型：
--
作者：
McBryant, SJ;Park, YJ;Luger, K
酵母核小体组装蛋白1（yNAP 1）参与许多不同的活动，例如将新合成的DNA组装成染色质和在转录激活期间核小体的重排。yNAP 1不需要ATP水解来执行这些功能，并且是体外染色质组装的有价值的工具。使用重组组蛋白复合物，我们表明，yNAP 1具有优先结合（H3-H4）（2）四聚体超过（H2 A-H2 B）二聚体。我们发现，组蛋白尾部的损失废除了这种偏好H3和H4，我们证明了一个直接的相互作用yNAP 1和H3和H4的氨基末端的尾巴。yNAP 1与一个组蛋白折叠结构域结合，从而指定与组蛋白二聚体和四聚体形成的复合物的化学计量。最后，我们提供的证据表明，酸性羧基末端区域的yNAP 1，虽然在体外组装的核小体，有助于通过结构独立的静电相互作用的结合。我们的研究结果是一致的，最近的NAP 1机制的调查，扩大了我们的理解组蛋白伴侣家庭的组装因子。
The yeast nucleosome assembly protein 1 (yNAP1) participates in many diverse activities, such as the assembly of newly synthesized DNA into chromatin and the rearrangement of nucleosomes during transcriptional activation. yNAP1 does not require ATP hydrolysis to perform these functions and is a valuable tool for in vitro chromatin assembly. Using recombinant histone complexes, we show that yNAP1 has a preference for binding the (H3-H4)(2) tetramer over the (H2A-H2B) dimer. We find that the loss of the histone tails abrogates this preference for H3 and H4, and we demonstrate a direct interaction between yNAP1 and the amino-terminal tails of H3 and H4. yNAP1 binds to one histone fold domain, thus specifying the stoichiometry of the complexes formed with the histone dimer and tetramer. Finally, we provide evidence that the acidic carboxyl-terminal region of yNAP1, although dispensable for nucleosome assembly in vitro, contributes to binding via structure-independent electrostatic interactions. Our results are consistent with recent mechanistic investigations of NAP1 and expand our understanding of the histone chaperone family of assembly factors.