Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel

Fujiwara, Yuichoiro; Takeshita, Kohei; Nakagawa, Atushi; Okamura, Yasushi

doi:https://doi.org/10.1074/jbc.M113.459024

アクセス数:199件（2024-10-10 04:37 集計）

固定URL: https://hdl.handle.net/11094/73662

閲覧可能ファイル

ファイル	フォーマット	利用条件	サイズ	閲覧回数	利用開始日	説明	information
JBC288_25_17968	pdf	なし	1.82 MB	144	2019.12.06

論文情報

ファイル出力

タイトル	Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel
著者	著者名 Fujiwara, Yuichoiro
	NRID 1000080346808 1000080346808 著者名 Takeshita, Kohei
	NRID 1000020188890 1000020188890 ORCID 0000-0002-1700-7861 0000-0002-1700-7861 researchmap permalink atsushi_nakagawa atsushi_nakagawa Scopus Author ID 7202934909 7202934909 著者名 Nakagawa, Atushi
	NRID 1000080201987 1000080201987 researchmap permalink yasushiokamura yasushiokamura Scopus Author ID 55322083200 55322083200 著者名 Okamura, Yasushi
内容	This research was originally published in Journal of Biological Chemistry. Yuichiro Fujiwara, Kohei Takeshita, Atsushi Nakagawa and Yasushi Okamura. Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel. Journal of Biological Chemistry. 2013; 288, 17968-17975. © the American Society for Biochemistry and Molecular Biology.
抄録	Oxidation is an important biochemical defense mechanism, but it also elicits toxicity; therefore, oxidation must be under strict control. In phagocytotic events in neutrophils, the voltagegated H^＋ (Hv) channel is a key regulator of the production of reactive oxygen species against invading bacteria. The cytoplasmic domain of the Hv channel forms a dimeric coiled coil underpinning a dimerized functional unit. Importantly, in the alignment of the coiled-coil core, a conserved cysteine residue forms a potential intersubunit disulfide bond. In this study, we solved the crystal structures of the coiled-coil domain in reduced, oxidized, and mutated (Cys → Ser) states. The crystal structures indicate that a pair of Cys residues forms an intersubunit disulfide bond dependent on the redox conditions. CD spectroscopy revealed that the disulfide bond increases the thermal stability of the coiled-coil protein. We also reveal that two thiol modifier molecules are able to bind to Cys in a redox-dependent manner without disruption of the dimeric coiled-coil assembly. Thus, the biochemical properties of the cytoplasmic coiled-coil domain in the Hv channel depend on the redox condition, which may play a role in redox sensing in the phagosome.
出版者	American Society for Biochemistry and Molecular Biology
収録物名	Journal of Biological Chemistry
巻(号)	288(25)
ページ	17968-17975
刊行年月	2013-06
言語	英語
ハンドルURL	https://hdl.handle.net/11094/73662
eISSN	1083351X
NCID	AA1202441X
関連情報 (isIdenticalTo)	DOI (出版社版) https://doi.org/10.1074/jbc.M113.459024
関連情報 (isIdenticalTo)	PMID 23667254
アクセス権	open access
権利情報	© the American Society for Biochemistry and Molecular Biology.
出版タイプ	Version of Record
カテゴリ	学術雑誌論文 Journal Article

資源タイプ	学術雑誌論文
ローカル資源タイプ	学術雑誌論文
DCMI資源タイプ	text
DCTERMS.bibliographicCitation	Journal of Biological Chemistry. 2013, 288(25), p. 17968-17975
DC.title	Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel
DC.creator	Fujiwara, Yuichoiro
	Takeshita, Kohei
	Nakagawa, Atushi
	Okamura, Yasushi
DC.publisher	American Society for Biochemistry and Molecular Biology
DC.language' scheme='DCTERMS.RFC1766	英語
DC.type' scheme='DCTERMS.DCMIType	text
DCTERMS.issued' scheme='DCTERMS.W3CDTF	2013-06
DC.identifier	https://doi.org/10.1074/jbc.M113.459024
DC.description	This research was originally published in Journal of Biological Chemistry. Yuichiro Fujiwara, Kohei Takeshita, Atsushi Nakagawa and Yasushi Okamura. Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel. Journal of Biological Chemistry. 2013; 288, 17968-17975. © the American Society for Biochemistry and Molecular Biology.
DCTERMS.abstract	Oxidation is an important biochemical defense mechanism, but it also elicits toxicity; therefore, oxidation must be under strict control. In phagocytotic events in neutrophils, the voltagegated H^＋ (Hv) channel is a key regulator of the production of reactive oxygen species against invading bacteria. The cytoplasmic domain of the Hv channel forms a dimeric coiled coil underpinning a dimerized functional unit. Importantly, in the alignment of the coiled-coil core, a conserved cysteine residue forms a potential intersubunit disulfide bond. In this study, we solved the crystal structures of the coiled-coil domain in reduced, oxidized, and mutated (Cys → Ser) states. The crystal structures indicate that a pair of Cys residues forms an intersubunit disulfide bond dependent on the redox conditions. CD spectroscopy revealed that the disulfide bond increases the thermal stability of the coiled-coil protein. We also reveal that two thiol modifier molecules are able to bind to Cys in a redox-dependent manner without disruption of the dimeric coiled-coil assembly. Thus, the biochemical properties of the cytoplasmic coiled-coil domain in the Hv channel depend on the redox condition, which may play a role in redox sensing in the phagosome.
DC.rights	© the American Society for Biochemistry and Molecular Biology.
DC.format	73662
citation_title	Structural characteristics of the redox-sensing coiled coil in the voltage-gated H^+ channel
citation_author	Fujiwara, Yuichoiro
	Takeshita, Kohei
	Nakagawa, Atushi
	Okamura, Yasushi
citation_publisher	American Society for Biochemistry and Molecular Biology
citation_language	英語
citation_date	2013-06
citation_journal_title	Journal of Biological Chemistry
citation_volume	288
citation_issue	25
citation_firstpage	17968
citation_lastpage	17975
citation_doi	https://doi.org/10.1074/jbc.M113.459024
citation_pmid	23667254
citation_public_url	https://hdl.handle.net/11094/73662

閲覧可能ファイル

論文情報

論文詳細を表示