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Dimeric Structure of the Blue Light Sensor Protein Photozipper in the Active State
http://hdl.handle.net/2237/00028327
http://hdl.handle.net/2237/00028327e1724cd2-253a-4a55-b4c8-ffd35e9c5200
名前 / ファイル | ライセンス | アクション |
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manuscriptPELDORforRep (410.8 kB)
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Item type | 学術雑誌論文 / Journal Article(1) | |||||
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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 | |||||
言語 | en | |||||
著者 |
Ozeki, Kohei
× Ozeki, Kohei× Tsukuno, Hiroyuki× Nagashima, Hiroki× Hisatomi, Osamu× Mino, Hiroyuki |
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アクセス権 | ||||||
アクセス権 | open access | |||||
アクセス権URI | http://purl.org/coar/access_right/c_abf2 | |||||
権利 | ||||||
言語 | en | |||||
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 | ||||||
内容記述タイプ | Abstract | |||||
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. | |||||
言語 | en | |||||
内容記述 | ||||||
内容記述タイプ | Other | |||||
内容記述 | ファイル公開:2019/02/06 | |||||
言語 | ja | |||||
出版者 | ||||||
出版者 | ACS Publications | |||||
言語 | en | |||||
言語 | ||||||
言語 | eng | |||||
資源タイプ | ||||||
資源タイプ識別子 | http://purl.org/coar/resource_type/c_6501 | |||||
資源タイプ | journal article | |||||
出版タイプ | ||||||
出版タイプ | AM | |||||
出版タイプResource | http://purl.org/coar/version/c_ab4af688f83e57aa | |||||
DOI | ||||||
関連タイプ | isVersionOf | |||||
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 | PISSN | |||||
収録物識別子 | 0006-2960 | |||||
書誌情報 |
en : Biochemistry 巻 57, 号 5, p. 494-497, 発行日 2018-02-06 |
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著者版フラグ | ||||||
値 | author |