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  1. B100 理学部/理学研究科
  2. B100a 雑誌掲載論文
  3. 学術雑誌

Dimeric Structure of the Blue Light Sensor Protein Photozipper in the Active State

http://hdl.handle.net/2237/00028327
e1724cd2-253a-4a55-b4c8-ffd35e9c5200
名前 / ファイル ライセンス アクション
manuscriptPELDORforRep.pdf manuscriptPELDORforRep (410.8 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2018-07-02
タイトル
タイトル Dimeric Structure of the Blue Light Sensor Protein Photozipper in the Active State
著者 Ozeki, Kohei

× Ozeki, Kohei

WEKO 78364

Ozeki, Kohei

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Tsukuno, Hiroyuki

× Tsukuno, Hiroyuki

WEKO 78365

Tsukuno, Hiroyuki

Search repository
Nagashima, Hiroki

× Nagashima, Hiroki

WEKO 78366

Nagashima, Hiroki

Search repository
Hisatomi, Osamu

× Hisatomi, Osamu

WEKO 78367

Hisatomi, Osamu

Search repository
Mino, Hiroyuki

× Mino, Hiroyuki

WEKO 78368

Mino, Hiroyuki

Search repository
権利
権利情報 “This document is the Accepted Manuscript version of a Published Work that appeared in final form in [Biochemistry], copyright © American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see [http://pubs.acs.org/articlesonrequest/AOR-3F5DaaWT3x2Ir9KDijgv].”
抄録
内容記述 The light oxygen voltage-sensing (LOV) domain plays a crucial role in blue light (BL) sensing in plants and microorganisms. LOV domains are usually associated with the effector domains and regulate the activities of effector domains in a BL-dependent manner. Photozipper (PZ) is monomeric in the dark state. BL induces reversible dimerization of PZ and subsequently increases its affinity for the target DNA sequence. In this study, we report the analyses of PZ by pulsed electron–electron double resonance (PELDOR). The neutral flavin radical was formed by BL illumination in the presence of dithiothreitol in the LOV-C254S (without the bZIP domain) and PZ-C254S mutants, where the cysteine residue responsible for adduct formation was replaced with serine. The magnetic dipole interactions of 3 MHz between the neutral radicals were detected in both LOV-C254S and PZ-C254S, indicating that these mutants are dimeric in the radical state. The PELDOR simulation showed that the distance between the radical pair is close to that estimated from the dimeric crystal structure in the “light state” [Heintz, U., and Schlichting, I. (2016) eLife 5, e11860], suggesting that in the radical state, LOV domains in PZ-C254S form a dimer similar to that of LOV-C254S, which lacks the bZIP domain.
内容記述タイプ Abstract
内容記述
内容記述 ファイル公開:2019/02/06
内容記述タイプ Other
出版者
出版者 ACS Publications
言語
言語 eng
資源タイプ
資源タイプresource http://purl.org/coar/resource_type/c_6501
タイプ journal article
DOI
関連識別子
識別子タイプ DOI
関連識別子 https://doi.org/10.1021/acs.biochem.7b01045
ISSN
収録物識別子タイプ ISSN
収録物識別子 0006-2960
書誌情報 Biochemistry

巻 57, 号 5, p. 494-497, 発行日 2018-02-06
著者版フラグ
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