Molecular Biophysics Unit, Indian Institute of Science, Bengaluru, India.
NMR Research Centre, Indian Institute of Science, Bengaluru, India.
FEBS Lett. 2019 Oct;593(19):2716-2729. doi: 10.1002/1873-3468.13540. Epub 2019 Aug 2.
AT-rich interaction domain (ARID)-containing BAF250a protein is a central DNA-binding subunit of the SWI/SNF chromatin-remodeling complex. ARIDs are found in several eukaryotic proteins that play roles in different aspects of cellular physiology. However, despite their biological importance, ARIDs remain relatively uncharacterized for their dynamics and DNA binding. Here, we have probed the structure and DNA-binding properties of BAF250a ARID. We show that the core BAF250a ARID interacts with DNA sequences with low micromolar affinities. NMR chemical shift perturbation (CSP) results reveal a number of conserved residues in ARID that are involved in DNA binding. An NMR CSP-based docking model of ARID-DNA complexes reveals that BAF250a ARID possesses necessary determinants of specific DNA binding.
富含 AT 的相互作用结构域（ARID）结合蛋白 BAF250a 是 SWI/SNF 染色质重塑复合物的核心 DNA 结合亚基。ARID 存在于几种真核蛋白中，这些蛋白在细胞生理的不同方面发挥作用。然而，尽管它们具有生物学重要性，但 ARID 对于其动力学和 DNA 结合仍然相对未被描述。在这里，我们探测了 BAF250a ARID 的结构和 DNA 结合特性。我们表明，核心 BAF250a ARID 以低微摩尔亲和力与 DNA 序列相互作用。NMR 化学位移扰动（CSP）结果揭示了 ARID 中涉及 DNA 结合的许多保守残基。基于 NMR CSP 的 ARID-DNA 复合物对接模型表明，BAF250a ARID 具有特定 DNA 结合的必要决定因素。
