Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
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<jats:title>Abstract</jats:title><jats:p>Cysteine hydropersulfide (CysSSH) occurs in abundant quantities in various organisms, yet little is known about its biosynthesis and physiological functions. Extensive persulfide formation is apparent in cysteine-containing proteins in <jats:italic>Escherichia coli</jats:italic> and mammalian cells and is believed to result from post-translational processes involving hydrogen sulfide-related chemistry. Here we demonstrate effective CysSSH synthesis from the substrate <jats:sc>l</jats:sc>-cysteine, a reaction catalyzed by prokaryotic and mammalian cysteinyl-tRNA synthetases (CARSs). Targeted disruption of the genes encoding mitochondrial CARSs in mice and human cells shows that CARSs have a crucial role in endogenous CysSSH production and suggests that these enzymes serve as the principal cysteine persulfide synthases in vivo. CARSs also catalyze co-translational cysteine polysulfidation and are involved in the regulation of mitochondrial biogenesis and bioenergetics. Investigating CARS-dependent persulfide production may thus clarify aberrant redox signaling in physiological and pathophysiological conditions, and suggest therapeutic targets based on oxidative stress and mitochondrial dysfunction.</jats:p>
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- Nature Communications
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Nature Communications 8 (1), 1177-, 2017-10
Nature Research
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詳細情報 詳細情報について
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- CRID
- 1050282677537321600
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- NII論文ID
- 120007134656
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- NII書誌ID
- AA12645905
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- ISSN
- 20411723
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- HANDLE
- 2241/00149118
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- 本文言語コード
- en
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- 資料種別
- journal article
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- データソース種別
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