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Five Amino Acid Residues Responsible for the High Stability of Hydrogenobacter thermophilus Cytochrome c552

https://hiroshima.repo.nii.ac.jp/records/2007232
https://hiroshima.repo.nii.ac.jp/records/2007232
e10e57f9-eb8a-4e31-82e5-ff57bd8de3c2
名前 / ファイル ライセンス アクション
J. J. Biol. Chem_280_5527.pdf (207.3 KB)
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 Five Amino Acid Residues Responsible for the High Stability of Hydrogenobacter thermophilus Cytochrome c552
言語 en
作成者 Oikawa, Kenta

× Oikawa, Kenta

en Oikawa, Kenta

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Nakamura, Shota

× Nakamura, Shota

en Nakamura, Shota

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Sonoyama, Takafumi

× Sonoyama, Takafumi

en Sonoyama, Takafumi

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Ohshima, Atsushi

× Ohshima, Atsushi

en Ohshima, Atsushi

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Kobayashi, Yuji

× Kobayashi, Yuji

en Kobayashi, Yuji

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Takayama, Shin-ichi J.

× Takayama, Shin-ichi J.

en Takayama, Shin-ichi J.

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Yamamoto, Yasuhiko

× Yamamoto, Yasuhiko

en Yamamoto, Yasuhiko

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Uchiyama, Susumu

× Uchiyama, Susumu

en Uchiyama, Susumu

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Hasegawa, Jun

× Hasegawa, Jun

en Hasegawa, Jun

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Sambongi, Yoshihiro

× Sambongi, Yoshihiro

en Sambongi, Yoshihiro

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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 This research was originally published in the Journal of Biological Chemistry. Kenta Oikawa, Shota Nakamura, Takafumi Sonoyama, Atsushi Ohshima, Yuji Kobayashi, Shin-ichi J. Takayama, Yasuhiko Yamamoto, Susumu Uchiyama, Jun Hasegawa, and Yoshihiro Sambongi. Five Amino Acid Residues Responsible for the High Stability of Hydrogenobacter thermophilus Cytochrome c552. J Biol Chem. 2005; 280:5527-5532. © 2005 the American Society for Biochemistry and Molecular Biology, Inc.
内容記述
内容記述 Five amino acid residues responsible for extreme stability have been identified in cytochrome c552 (HT c552) from a thermophilic bacterium, Hydrogenobacter thermophilus. The five residues, which are spatially distributed in three regions of HT c552, were replaced with the corresponding residues in the homologous but less stable cytochrome c551 (PA c551) from Pseudomonas aeruginosa. The quintuple HT c552 variant (A7F/M13V/Y34F/Y43E/I78V) showed the same stability against guanidine hydrochloride denaturation as that of PA c551, suggesting that the five residues in HT c552 necessarily and sufficiently contribute to the overall stability. In the three HT c552 variants carrying mutations in each of the three regions, the Y34F/Y43E mutations resulted in the greatest destabilization, by –13.3 kJ mol–1, followed by A7F/M13V (–3.3 kJ mol–1) and then I78V (–1.5 kJ mol–1). The order of destabilization in HT c552 was the same as that of stabilization in PA c551 with reverse mutations such as F34Y/E43Y, F7A/V13M, and V78I (13.4, 10.3, and 0.3 kJ mol–1, respectively). The results of guanidine hydrochloride denaturation were consistent with those of thermal denaturation for the same variants. The present study established a method for reciprocal mutation analysis. The effects of side-chain contacts were experimentally evaluated by swapping the residues between the two homologous proteins that differ in stability. A comparative study of the two proteins was a useful tool for assessing the amino acid contribution to the overall stability.
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 from Hiroshima University, the Noda Institute for Scientific Research, and the Japanese Ministry of Education, Science and Culture (grants-in-aid for Scientific Research on Priority Areas).
出版者
出版者 The American Society for Biochemistry and Molecular Biology, 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 VoR
出版タイプResource http://purl.org/coar/version/c_970fb48d4fbd8a85
関連情報
識別子タイプ DOI
関連識別子 10.1074/jbc.M412392200
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M412392200
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 0021-9258
収録物識別子
収録物識別子タイプ ISSN
収録物識別子 1083-351X
開始ページ
開始ページ 5527
書誌情報 Journal of Biological Chemistry
Journal of Biological Chemistry

巻 280, 号 7, p. 5527-5532, 発行日 2005-02-18
旧ID 48773
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