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首页> 外文期刊>Journal of Molecular Biology >A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1
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A beta-hairpin comprising the nuclear localization sequence sustains the self-associated states of nucleosome assembly protein 1

机译：包含核定位序列的β-发夹维持核小体组装蛋白1的自缔合状态。

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摘要

The histone chaperone nucleosome assembly protein 1 (NAP1) is implicated in histone shuttling as well as nucleosome assembly and disassembly. Under physiological conditions, NAP1 dimers exist in a mixture of various high-molecular-weight oligomers whose size may be regulated by the cell cycle-dependent concentration of NAP1. Both the functional and structural significance of the observed oligomers are unknown. We have resolved the molecular mechanism by which yeast NAP1 (yNAP1) dimers oligomerize by applying x-ray crystallographic, hydrodynamic, and functional approaches. We found that an extended beta-hairpin that protrudes from the compact core of the yNAP1 dimer forms a stable beta-sheet with beta-hairpins of neighboring yNAP1 dimers. Disruption of the beta-hairpin (whose sequence is conserved among NAP1 proteins in various species) by the replacement of one or more amino acids with proline results in complete loss of yNAP1 dimer oligomerization. The in vitro functions of yNAP1 remain unaffected by the mutations. We have thus identified a conserved structural feature of NAP1 whose function, in addition to presenting the nuclear localization sequence, appears to be the formation of higher-order oligomers. (c) 2007 Elsevier Ltd. All rights reserved.
机译：组蛋白伴侣核小体组装蛋白1（NAP1）与组蛋白穿梭以及核小体组装和拆卸有关。在生理条件下，NAP1二聚体存在于各种高分子量低聚物的混合物中，其大小可能受细胞周期依赖性NAP1浓度的调节。所观察到的低聚物的功能和结构意义均未知。我们已经通过应用X射线晶体学，流体力学和功能方法解决了酵母NAP1（yNAP1）二聚体寡聚的分子机制。我们发现，从yNAP1二聚体的紧密核心突出的扩展β-发夹与相邻yNAP1二聚体的β-发夹形成了稳定的β-折叠。通过用脯氨酸替换一个或多个氨基酸来破坏β-发夹结构（其序列在各种物种的NAP1蛋白之间是保守的）导致yNAP1二聚体寡聚完全丧失。 yNAP1的体外功能保持不受突变的影响。因此，我们确定了NAP1的保守结构特征，其功能除了提供核定位序列外，还似乎是高阶寡聚物的形成。 （c）2007 Elsevier Ltd.保留所有权利。

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