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  1. B300 農学部/生命農学研究科
  2. B300a 雑誌掲載論文
  3. 学術雑誌

Oligomerization of H+-pyrophosphatase and its structural and functional consequences

http://hdl.handle.net/2237/6661
http://hdl.handle.net/2237/6661
4bf69973-9e69-48f4-b0c3-9e9e7f448d82
名前 / ファイル ライセンス アクション
2005-BBA-ScPP.pdf 2005-BBA-ScPP.pdf (918.3 kB)
Item type 学術雑誌論文 / Journal Article(1)
公開日 2006-06-30
タイトル
タイトル Oligomerization of H+-pyrophosphatase and its structural and functional consequences
言語 en
著者 Mimura, Hisatoshi

× Mimura, Hisatoshi

WEKO 12640

en Mimura, Hisatoshi

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Nakanishi, Yoichi

× Nakanishi, Yoichi

WEKO 12641

en Nakanishi, Yoichi

Search repository
Maeshima, Masayoshi

× Maeshima, Masayoshi

WEKO 12642

en Maeshima, Masayoshi

Search repository
前島, 正義

× 前島, 正義

WEKO 12643

ja 前島, 正義

Search repository
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
キーワード
主題Scheme Other
主題 Disulfide bond
キーワード
主題Scheme Other
主題 H+-pyrophosphatase
キーワード
主題Scheme Other
主題 Oligomerization
キーワード
主題Scheme Other
主題 Proton pump
抄録
内容記述 The H+-pyrophosphatase (H+-PPase) consists of a single polypeptide, containing 16 or 17 transmembrane domains. To determine the higher order oligomeric state of Streptomyces coelicolor H+-PPase, we constructed a series of cysteine substitution mutants and expressed them in Escherichia coli. Firstly, we analyzed the formation of disulfide bonds, promoted by copper, in mutants with single cysteine substitutions. 28 of 39 mutants formed disulfide bonds, including S545C, a substitution at the periplasmic side. The formation of intermolecular disulfide bonds suppressed the enzyme activity of several, where the substituted residues were located in the cytosol. Creating disulfide links in the cytosol may interfere with the enzyme’s catalytic function. Secondly, we prepared double mutants by introducing second cysteine substitutions into the S545C mutant. These double-cysteine mutants produced cross-linked complexes, estimated to be at least tetramers and possibly hexamers. Thirdly, we co-expressed epitope-tagged, wild type and inactive mutant H+-PPases in E. coli and confirmed the formation of oligomers by co-purifying one subunit using the epitope tag used to label the other. The enzyme activity of these oligomers was markedly suppressed. We propose that H+-PPase is present as an oligomer made up of at least two or three sets of dimers.
言語 en
内容記述タイプ Abstract
出版者
言語 en
出版者 Elsevier
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
出版タイプ
出版タイプ VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
書誌情報 en : Biochimica et Biophysica Acta

巻 1708, 号 3, p. 393-403, 発行日 2005-07
フォーマット
application/pdf
著者版フラグ
値 publisher
URI
識別子 http://hdl.handle.net/2237/6661
識別子タイプ HDL
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