DNA结合蛋白

DNA结合蛋白（DNA-binding protein）是指能透过DNA结合结构域（英语：DNA-binding domain）（DBD）与单链或双链DNA结合的一类蛋白质。一般来说，能与特异DNA序列结合的DNA结合蛋白主要经由与B-DNA（生物体内DNA一般都是B-DNA形式）的大沟结合来识别DNA序列。因为B-DNA的大沟区域能容许更多蛋白质上的官能团靠近并与之进行相互作用。 蛋白质与DNA的结合受到pH值、温度、离子强度、电场，以及大分子拥挤（英语：Macromolecular crowding）等多种条件的影响，具体分为特异性与非特异性两种。非特异性的结合指蛋白质与DNA的结合不依赖特定序列，而特异性的结合则只会发生在特定的DNA序列上。在Cas9/CRSIPER系统出现前作为主流基因编辑工具的锌指蛋白以及TALENs都是依赖特异性的DNA蛋白间结合工作的。 较早期的检测蛋白与DNA间相互作用的方法包括凝胶迁移实验（EMSA）、DNA-蛋白质相互作用ELISA实验（DPI-ELISA）、DNA酶足迹法（英语：DNase footprinting assay）（DNase footprinting assay） 等等。而染色质免疫沉淀法（ChIP）则是目前较为通行的检测体内DNA与蛋白质相互作用的方法。 最常见的一种非特异性DNA结合蛋白是真核生物染色质中与DNA结合的组蛋白。组蛋白主要是通过所带的正电荷与带负电的DNA结合，所以组蛋白与DNA之间的结合不依赖DNA上的特定序列。这也符合组蛋白的生物学功能，因为组蛋白需要与各种不同的DNA片段结合形成染色质的基本组成单位核小体。另外，真核生物染色质上能够使DNA链发生弯曲的高迁移率族（HMG）蛋白与DNA之间的结合也是非特异性的。 很多特异性DNA结合蛋白属于转录因子。转录因子依赖其特有的DNA结合结构域与DNA上的特定序列结合。一般来说，转录因子在与DNA结合后，会招募酶对DNA或组蛋白进行修饰，进而调控基因的表达水平。 内切酶 蛋白质相互作用 Travers, A. A. DNA-protein interactions. London: Springer. 1993. ISBN 978-0-412-25990-6.  Pabo CO, Sauer RT. 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