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Mitochondria-specific RNA-modifying Enzymes Responsible for the Biosynthesis of the Wobble Base in Mitochondrial tRNAs

https://hiroshima.repo.nii.ac.jp/records/2007231
https://hiroshima.repo.nii.ac.jp/records/2007231
3c3c7929-f798-4129-afb6-87eaab441bc3
名前 / ファイル ライセンス アクション
J. J. Biol. Chem._280_1613.pdf (1.4 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 Mitochondria-specific RNA-modifying Enzymes Responsible for the Biosynthesis of the Wobble Base in Mitochondrial tRNAs
言語 en
作成者 Umeda, Noriko

× Umeda, Noriko

en Umeda, Noriko

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Suzuki, Takeo

× Suzuki, Takeo

en Suzuki, Takeo

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Yukawa, Masashi

× Yukawa, Masashi

en Yukawa, Masashi

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Ohya, Yoshikazu

× Ohya, Yoshikazu

en Ohya, Yoshikazu

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Shindo, Heisaburo

× Shindo, Heisaburo

en Shindo, Heisaburo

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Watanabe, Kimitsuna

× Watanabe, Kimitsuna

en Watanabe, Kimitsuna

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Suzuki, Tsutomu

× Suzuki, Tsutomu

en Suzuki, Tsutomu

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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. Noriko Umeda, Takeo Suzuki, Masashi Yukawa, Yoshikazu Ohya, Heisaburo Shindo, Kimitsuna Watanabe, and Tsutomu Suzuki. Mitochondria-specific RNA-modifying Enzymes Responsible for the Biosynthesis of the Wobble Base in Mitochondrial tRNAs. J Biol Chem. 2005; 280:1613-1624. © 2005 by The American Society for Biochemistry and Molecular Biology, Inc.
内容記述
内容記述 Human mitochondrial (mt) tRNALys has a taurine-containing modified uridine, 5-taurinomethyl-2-thiouridine (τm5s2U), at its anticodon wobble position. We previously found that the mt tRNALys, carrying the A8344G mutation from cells of patients with myoclonus epilepsy associated with ragged-red fibers (MERRF), lacks the τm5s2U modification. Here we describe the identification and characterization of a tRNA-modifying enzyme MTU1 (mitochondrial tRNA-specific 2-thiouridylase 1) that is responsible for the 2-thiolation of the wobble position in human and yeast mt tRNAs. Disruption of the yeast MTU1 gene eliminated the 2-thio modification of mt tRNAs and impaired mitochondrial protein synthesis, which led to reduced respiratory activity. Furthermore, when MTO1 or MSS1, which are responsible for the C5 substituent of the modified uridine, was disrupted along with MTU1, a much more severe reduction in mitochondrial activity was observed. Thus, the C5 and 2-thio modifications act synergistically in promoting efficient cognate codon decoding. Partial inactivation of MTU1 in HeLa cells by small interference RNA also reduced their oxygen consumption and resulted in mitochondria with defective membrane potentials, which are similar phenotypic features observed in MERRF.
言語 en
内容記述
内容記述タイプ Other
内容記述 This work was supported by grants-in-aid for scientific research on priority areas from the Ministry of Education, Science, Sports, and Culture of Japan, and by a grant from the New Energy and Industrial Technology Development Organization (to T. S.).
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.M409306200
関連情報
識別子タイプ DOI
関連識別子 https://doi.org/10.1074/jbc.M409306200
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 1613
書誌情報 Journal of Biological Chemistry
Journal of Biological Chemistry

巻 280, 号 2, p. 1613-1624, 発行日 2005-01-14
旧ID 48781
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