Cys redox reactions and metal binding of a CYS2His2 zinc finger
Cys redox reactions and metal binding of a CYS2His2 zinc finger
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DOI：
10.1016/j.abb.2004.10.024
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发表时间：
2005-02-01
影响因子：
3.9
通讯作者：
Hanas, JS
中科院分区：
文献类型：
--
作者：
Larabee, JL;Hocker, JR;Hanas, JS
阐明半胱氨酸（Cys）氧化还原反应影响金属与锌指结构域结合的机制对于理解锌指的结构和功能非常重要。目前的研究利用电喷雾电离质谱 (ESI-MS) 来分析 Cys 氧化还原反应及其对金属离子与合成多肽结合的影响，该合成多肽的基序与 RNA 聚合酶 II 转录因子 Sp1 (Sp1-3) 的第三个锌指相似。在一系列氧化还原改变的二硫苏糖醇、过氧化氢和氢离子浓度范围内，证明了金属与该锌指结构域的结合事件的差异特异性。通过使用 ESI-MS 以单 Da 分辨率分析此 Cys(2)His(2) 锌指结构域，天然同位素簇的变化表明 Cys 硫醇和硫醇盐可有助于 Zn2+ 和其他金属离子的配位。这些实验提供了对 Cys(2)His(2) 锌指结构域的基本氧化还原化学和金属结合机制的深入了解。 (C) 2004 Elsevier Inc. 保留所有权利。
The elucidation of mechanisms by which cysteine (Cys) redox reactions influence metal binding to zinc finger domains is important for understanding the structure and function of zinc fingers. The present studies utilize electrospray ionization mass spectrometry (ESI-MS) to analyze Cys redox reactions and their influence on metal ion binding to a synthetic polypeptide similar in motif to the third zinc finger of the RNA polymerase II transcription factor, Sp1 (Sp1-3). The differential specificity of metal binding events to this zinc finger domain is demonstrated over a range of redox-altering dithiothreitol, hydrogen peroxide, and hydrogen ion concentrations. By analyzing this Cys(2)His(2) zinc finger domain at single Da resolution with ESI-MS, shifts in the natural isotope cluster demonstrate that a Cys thiol and thiolate can contribute to Zn2+ and other metal ion coordination. These experiments provide insight into the basic redox chemistry and metal binding mechanisms of Cys(2)His(2) zinc finger domains. (C) 2004 Elsevier Inc. All rights reserved.