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突出 MBP 结晶伴侣在拟南芥 BIL1/BZR1 转录因子-DNA 复合物中的潜在应用。

Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex.

机构信息

Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Tokyo, 113-8657, Japan.

Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, 113-8657, Japan.

出版信息

Sci Rep. 2021 Feb 16;11(1):3879. doi: 10.1038/s41598-021-83532-2.

DOI:10.1038/s41598-021-83532-2
PMID:33594119
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7887268/
Abstract

The maltose-binding protein (MBP) fusion tag is one of the most commonly utilized crystallization chaperones for proteins of interest. Recently, this MBP-mediated crystallization technique was adapted to Arabidopsis thaliana (At) BRZ-INSENSITIVE-LONG (BIL1)/BRASSINAZOLE-RESISTANT (BZR1), a member of the plant-specific BZR TFs, and revealed the first structure of AtBIL1/BZR1 in complex with target DNA. However, it is unclear how the fused MBP affects the structural features of the AtBIL1/BZR1-DNA complex. In the present study, we highlight the potential utility of the MBP crystallization chaperone by comparing it with the crystallization of unfused AtBIL1/BZR1 in complex with DNA. Furthermore, we assessed the validity of the MBP-fused AtBIL1/BZR1-DNA structure by performing detailed dissection of crystal packings and molecular dynamics (MD) simulations with the removal of the MBP chaperone. Our MD simulations define the structural basis underlying the AtBIL1/BZR1-DNA assembly and DNA binding specificity by AtBIL1/BZR1. The methodology employed in this study, the combination of MBP-mediated crystallization and MD simulation, demonstrates promising capabilities in deciphering the protein-DNA recognition code.

摘要

麦芽糖结合蛋白（MBP）融合标签是最常用于目标蛋白的结晶伴侣之一。最近，这种 MBP 介导的结晶技术被应用于拟南芥（At）BRZ-INSENSITIVE-LONG（BIL1）/BRASSINAZOLE-RESISTANT（BZR1），一种植物特异性 BZR TF 的成员，并揭示了 AtBIL1/BZR1 与靶 DNA 复合物的第一个结构。然而，融合的 MBP 如何影响 AtBIL1/BZR1-DNA 复合物的结构特征尚不清楚。在本研究中，我们通过比较融合 MBP 的 AtBIL1/BZR1 与 DNA 复合物的结晶，突出了 MBP 结晶伴侣的潜在用途。此外，我们通过去除 MBP 伴侣进行晶体堆积和分子动力学（MD）模拟的详细剖析，评估了 MBP 融合的 AtBIL1/BZR1-DNA 结构的有效性。我们的 MD 模拟通过 AtBIL1/BZR1 定义了 AtBIL1/BZR1-DNA 组装和 DNA 结合特异性的结构基础。本研究中采用的方法，即 MBP 介导的结晶和 MD 模拟的结合，展示了在破译蛋白-DNA 识别密码方面的有前途的能力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/73d5ae370d48/41598_2021_83532_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/550b6f523d5f/41598_2021_83532_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/c1c819fe4ace/41598_2021_83532_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/b124baef278c/41598_2021_83532_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/e66805ee578f/41598_2021_83532_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/73d5ae370d48/41598_2021_83532_Fig5_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/550b6f523d5f/41598_2021_83532_Fig1_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/c1c819fe4ace/41598_2021_83532_Fig2_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/b124baef278c/41598_2021_83532_Fig3_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/e66805ee578f/41598_2021_83532_Fig4_HTML.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/388e/7887268/73d5ae370d48/41598_2021_83532_Fig5_HTML.jpg

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