Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.
Binding kinetics of histone chaperone Chz1 and variant histone H2A.Z-H2B by relaxation dispersion NMR spectroscopy.
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通过弛豫分散核磁共振波谱研究组蛋白伴侣 Chz1 和变体组蛋白 H2A.Z-H2B 的结合动力学。
DOI：
10.1016/j.jmb.2009.01.009
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发表时间：
2009-03-20
影响因子：
5.6
通讯作者：
Kay, Lewis E.
中科院分区：
文献类型：
--
作者：
Hansen, D. Flemming;Zhou, Zheng;Fen, Haniqiao;Jenkins, Lisa M. Miller;Bai, Yawen;Kay, Lewis E.
真核细胞的基因组被包装成一种称为染色质的紧凑结构，由 DNA 以及组蛋白和非组蛋白组成。组蛋白伴侣与组蛋白相关，在细胞中染色质结构的组装和组蛋白的运输中发挥重要作用。最近发现的组蛋白伴侣 Chz1 与芽殖酵母的变体组蛋白 H2A.Z 相关，并在经典组蛋白对 H2A-H2B 与变体 H2A.Z-H2B 的交换中发挥关键作用。在这里，我们提出了一种 NMR 方法，可以准确估计 Chz1 和 H2A.Z-H2B 的结合和解离速率。该方法利用了这样一个事实：在 Chz1 和 H2A.Z-H2B 的 1:1 混合物中，光谱中不可见的少量未结合蛋白质会产生来自复合物的信号线展宽，这些信号可以根据交换过程的热力学和动力学进行量化。测得的解离速率常数 22±2 s−1 提供了 H2A.Z-H2B 向染色质重塑复合物转移速率的上限，而比扩散关联速率更快的 108±107 M−1s−1 则确定了形成伴侣：组蛋白复合物的吸引静电相互作用的重要性。
The genome of eukaryotic cells is packed into a compact structure called chromatin that consists of DNA as well as both histone and non-histone proteins. Histone-chaperones associate with histone proteins and play important roles in the assembly of chromatin structure and transport of histones in the cell. The recently discovered histone-chaperone Chz1 associates with the variant histone H2A.Z of budding yeast and plays a critical role in the exchange of the canonical histone pair H2A-H2B for the variant H2A.Z-H2B. Here, we present an NMR approach that provides accurate estimates for the rates of association and dissociation of Chz1 and H2A.Z-H2B. The methodology exploits the fact that in a 1:1 mixture of Chz1 and H2A.Z-H2B the small amounts of unbound proteins that are invisible in spectra produce line-broadening of signals from the complex that can be quantified in terms of the thermodynamics and kinetics of the exchange process. The dissociation rate constant measured, 22±2 s−1, provides an upper bound for the rate of transfer of H2A.Z-H2B to the chromatin remodeling complex and the faster than diffusion association rate, 108±107 M−1s−1, establishes the importance of attractive electrostatic interactions that form the chaperone:histone complex.
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