Association States of Nucleosome Assembly Protein 1 and Its Complexes with Histones*
Association States of Nucleosome Assembly Protein 1 and Its Complexes with Histones*
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DOI：
10.1074/jbc.m413329200
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发表时间：
2005-04
影响因子：
4.8
通讯作者：
K. Toth;J. Mazurkiewicz;K. Rippe
中科院分区：
文献类型：
--
作者：
K. Toth;J. Mazurkiewicz;K. Rippe
组蛋白伴侣NAP 1是组蛋白在核输入、核小体组装和染色质重塑过程中的载体。分析超离心用于确定NAP 1单独和与核心组蛋白复合物的缔合状态。此外，通过测定不同NAP 1物种之间的平衡解离常数来量化缔合的浓度依赖性。在生理蛋白质和盐浓度下，主要的种类是NAP 1二聚体和八聚体。这些也是发现以每个组蛋白一个NAP 1单体的化学计量与组蛋白相互作用的缔合状态。基于这些结果，提出了一个NAP 1二聚体-八聚体平衡的细胞周期依赖性移位模型，该模型反映了NAP 1的不同生物学功能。
The histone chaperone NAP1 is a carrier of histones during nuclear import, nucleosome assembly, and chromatin remodeling. Analytical ultracentrifugation was used to determine the association states of NAP1 alone and in complexes with core histones. In addition, the concentration dependence of the association was quantified by determining the equilibrium dissociation constant between different NAP1 species. At physiological protein and salt concentrations the prevalent species were the NAP1 dimer and octamer. These were also the association states found to interact with histones in a stoichiometry of one NAP1 monomer per histone. Based on these results a model for a cell cycle-dependent shift of the NAP1 dimer-octamer equilibrium is proposed that reflects different biological functions of NAP1.