核小体结合 PZP 结构域的结构和生物物理特性分析。
Structural and biophysical characterization of the nucleosome-binding PZP domain.
机构信息
Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.
Department of Physics, Ohio State University, Columbus, OH 43210, USA.
出版信息
STAR Protoc. 2021 Apr 19;2(2):100479. doi: 10.1016/j.xpro.2021.100479. eCollection 2021 Jun 18.
The core subunit of the MORF acetyltransferase complex BRPF1 contains a unique combination of zinc fingers, including a plant homeodomain (PHD) finger followed by a zinc knuckle and another PHD finger, which together form a PZP domain (BRPF1). BRPF1 has been shown to bind to the nucleosome and make contacts with both histone H3 tail and DNA. Here, we describe biophysical and structural methods for characterization of the interactions between BRPF1, H3 tail, DNA, and the intact nucleosome. For complete details on the use and execution of this protocol, please refer to Klein et al. (2020).
MORF 乙酰转移酶复合物的核心亚基 BRPF1 包含独特的锌指组合，包括一个植物同源结构域 (PHD) 手指，后面跟着一个锌指和另一个 PHD 手指，共同构成一个 PZP 结构域 (BRPF1)。已经表明，BRPF1 与核小体结合，并与组蛋白 H3 尾部和 DNA 接触。在这里，我们描述了用于表征 BRPF1、H3 尾部、DNA 和完整核小体之间相互作用的生物物理和结构方法。有关该方案使用和执行的完整详细信息，请参阅 Klein 等人。（2020 年）。
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