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  1. 010 学術雑誌論文
  2. 渡辺, 正勝 / WATANABE, Masakatsu

Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis

https://ir.soken.ac.jp/records/3884
https://ir.soken.ac.jp/records/3884
12214d1a-03e5-4f89-a04b-6c27931da792
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b505792b.pdf b505792b (271.0 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2013-08-13
タイトル
タイトル Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis
タイトル
タイトル Photocycle features of heterologously expressed and assembled eukaryotic flavin-binding BLUF domains of photoactivated adenylyl cyclase (PAC), a blue-light receptor in Euglena gracilis
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
著者 ITO, Shinji

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ITO, Shinji

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MURAKAMI, Akio

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MURAKAMI, Akio

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SATO, Kyosuke

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SATO, Kyosuke

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NISHINA, Yasuzo

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NISHINA, Yasuzo

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SHIGA, Kiyoshi

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SHIGA, Kiyoshi

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TAKAHASHI, Tetsuo

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TAKAHASHI, Tetsuo

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HIGASHI, Shoichi

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HIGASHI, Shoichi

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ISEKI, Mineo

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ISEKI, Mineo

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WATANABE, Masakatsu

× WATANABE, Masakatsu

WATANABE, Masakatsu

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著者別名 渡辺, 正勝

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渡辺, 正勝

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内容記述タイプ Abstract
内容記述 Photoactivated adenylyl cyclase (PAC) is a recently discovered blue-light photoreceptor that mediates photomovement in Euglena gracilis (Iseki et al., Nature, 2002, 415, 1047-1051). PAC appears to be a heterotetramer composed of two FAD-binding subunits (PACα and PACβ). Both subunits have a pair of homologous regions (F1 and F2) which show homology with prokaryotic "sensors of blue-light using FAD" (BLUF) domains. The F1 and F2 domains of PAC are the only eukaryotic BLUF domains found thus far. We obtained soluble recombinant F1 and F2 proteins in PACα by heterologous expression with fused glutathione-S-transferase (GST) in E. coli. The expressed F1 samples did not bind flavins, but the F2 samples contained both FAD and FMN with trace amounts of riboflavin. We also assembled the histidine-tagged recombinant F2 (6His-F2) from inclusion bodies in E. coli with exogenous FAD or FMN. Blue-light-induced changes in absorption spectra of these assembled samples were highly similar to those reported for prokaryotic BLUF domains. The FAD- or FMN-assembled 6His-F2 photocycled with nearly the same rate constants of light-reaction and dark-relaxation, which were slightly lower than those of GST-cleaved F2. The estimated quantum efficiency for the phototransformation was 0.28-0.32, and the half-life was 34-44 s at 25 °C for the recombinant PACα F2, whereas that reported for prokaryotic BLUF domains varied from ca. 3.5 s (Tl10078) to ca. 900 s (AppA). The mutated recombinant Y472F and Q514G of PACα F2 and the F2 domain of the PACα homologue from Eutreptiella gymnastica, which lacks the Gln residue conserved in other BLUF domains, showed no photoinduced transformation.
書誌情報 Photochemical and Photobiological Sciences
en : Photochemical and Photobiological Sciences

巻 4, 号 9, p. 762-769, 発行日 2005-09
出版者
出版者 Royal Society of Chemistry
ISSN
収録物識別子タイプ ISSN
収録物識別子 1474905X
PubMed番号
関連タイプ isIdenticalTo
識別子タイプ PMID
関連識別子 16121289
DOI
関連タイプ isIdenticalTo
識別子タイプ DOI
関連識別子 http://doi.org/10.1039/b505792b
関連名称 10.1039/b505792b
権利
権利情報 © The Royal Society of Chemistry and Owner Societies 2005
関連サイト
識別子タイプ URI
関連識別子 http://www.rsc.org/AboutUs/Copyright/LicencetoPublishforjournals.asp
関連名称 Copyright
フォーマット
内容記述タイプ Other
内容記述 application/pdf
著者版フラグ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
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