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Metal-binding domains and the metal selectivity of the vanadium(IV)-binding protein VBP-129 in blood plasma

https://hiroshima.repo.nii.ac.jp/records/2007358
https://hiroshima.repo.nii.ac.jp/records/2007358
741f04f7-309b-4d4d-a093-f035697d1f92
名前 / ファイル ライセンス アクション
JInorgBiochem_116_70.pdf JInorgBiochem_116_70.pdf (1.0 MB)
Item type デフォルトアイテムタイプ_(フル)(1)
公開日 2023-03-18
タイトル
タイトル Metal-binding domains and the metal selectivity of the vanadium(IV)-binding protein VBP-129 in blood plasma
言語 en
作成者 Ueki, Tatsuya

× Ueki, Tatsuya

en Ueki, Tatsuya

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Nakagawa, Takafumi

× Nakagawa, Takafumi

en Nakagawa, Takafumi

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Michibata, Hitoshi

× Michibata, Hitoshi

en Michibata, Hitoshi

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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
権利情報
権利情報 Copyright (c) 2012 Elsevier Inc. All rights reserved.
権利情報
権利情報 This manuscript version is made available under the CC-BY-NC-ND 4.0 license http://creativecommons.org/licenses/by-nc-nd/4.0/
主題
主題Scheme Other
主題 Vanadium
主題
主題Scheme Other
主題 Ascidian
主題
主題Scheme Other
主題 Metal-binding Protein
主題
主題Scheme Other
主題 Site-directed mutagenesis
主題
主題Scheme NDC
主題 460
内容記述
内容記述 Ascidians are well known to accumulate extremely high levels of vanadium in their blood cells. Several key proteins related to vanadium accumulation and physiological function have been isolated from vanadium-rich ascidians. Of these, vanadium(IV)-binding protein-129 (VBP-129) is a unique protein that has been identified from the blood plasma of an ascidian Ascidia sydneiensis samea, but its metal binding domains are not known. In this study, several deletion and point mutants of VBP-129 were generated, and their metal binding abilities were assessed by immobilized metal ion affinity chromatography (IMAC) and electron spin resonance spectroscopy (ESR). The internal partial protein, VBP-Int41, did not bind to VIV, but the two constructs, VBP-N52 and VBP-Int55, added with additional 11 or 14 neighboring amino acids bound to VIV. Mutations for cysteine-47 and lysine-50 in VBP-Int55 diminished VIV-binding in VBP-Int55, suggesting that these amino acid residues play important roles in binding VIV. ESR titration analysis revealed that VBP-129, VBP-N52 and VBP-Int55 could bind to 6, 3 and 2 VIV ions, respectively. ESR spectrum analysis indicated a N2O2 coordination geometry, which is similar to Vanabins. The cysteines may contribute to the maintenance of the three-dimensional structure that is necessary for binding VIV ions. VBP-129 did not have a VV-reductase activity, as expected from its tissue localization in blood plasma. This study provided the evidences that VBP-129 possesses VIV-binding domains that make a similar coordination to VIV as those by Vanabins but VBP-129 acts solely as VIV-chaperon in blood plasma.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported in part by Grants-in-Aid from the Ministry of Education, Culture, Sports, Science and Technology, Japan (nos. 20570070 and 21570077).
出版者
出版者 Elsevier Inc.
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 AO
出版タイプResource http://purl.org/coar/version/c_b1a7d7d4d402bcce
関連情報
識別子タイプ DOI
関連識別子 10.1016/j.jinorgbio.2012.08.003
関連情報
関連タイプ isVersionOf
識別子タイプ DOI
関連識別子 http://doi.org/10.1016/j.jinorgbio.2012.08.003
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0162-0134
収録物識別子
収録物識別子タイプ NCID
収録物識別子 AA00258264
開始ページ
開始ページ 70
書誌情報 Journal of Inorganic Biochemistry
Journal of Inorganic Biochemistry

巻 116, p. 70-76, 発行日 2012-11
旧ID 39964
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