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

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...

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Autores principales:	Shohei Nosaki, Tohru Terada, Akira Nakamura, Kei Hirabayashi, Yuqun Xu, Thi Bao Chau Bui, Takeshi Nakano, Masaru Tanokura, Takuya Miyakawa
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/60fe3a9e02344572974f25db0283195a
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spelling	oai:doaj.org-article:60fe3a9e02344572974f25db0283195a2021-12-02T12:11:17ZHighlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex10.1038/s41598-021-83532-22045-2322https://doaj.org/article/60fe3a9e02344572974f25db0283195a2021-02-01T00:00:00Zhttps://doi.org/10.1038/s41598-021-83532-2https://doaj.org/toc/2045-2322Abstract 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.Shohei NosakiTohru TeradaAkira NakamuraKei HirabayashiYuqun XuThi Bao Chau BuiTakeshi NakanoMasaru TanokuraTakuya MiyakawaNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-9 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Shohei Nosaki Tohru Terada Akira Nakamura Kei Hirabayashi Yuqun Xu Thi Bao Chau Bui Takeshi Nakano Masaru Tanokura Takuya Miyakawa Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
description	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.
format	article
author	Shohei Nosaki Tohru Terada Akira Nakamura Kei Hirabayashi Yuqun Xu Thi Bao Chau Bui Takeshi Nakano Masaru Tanokura Takuya Miyakawa
author_facet	Shohei Nosaki Tohru Terada Akira Nakamura Kei Hirabayashi Yuqun Xu Thi Bao Chau Bui Takeshi Nakano Masaru Tanokura Takuya Miyakawa
author_sort	Shohei Nosaki
title	Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
title_short	Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
title_full	Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
title_fullStr	Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
title_full_unstemmed	Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex
title_sort	highlighting the potential utility of mbp crystallization chaperone for arabidopsis bil1/bzr1 transcription factor-dna complex
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/60fe3a9e02344572974f25db0283195a
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Highlighting the potential utility of MBP crystallization chaperone for Arabidopsis BIL1/BZR1 transcription factor-DNA complex

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