Faculty Information |
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Article types | Original article |
Language | English |
Refereed paper | Refereed |
Title | Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics. |
Journal | Formal name:Nature communications Abbreviation:Nat Commun ISSN code:2041-1723(Electronic)2041-1723(Linking) |
Domestic / Foregin | Foregin |
Volume, Number, Page | 8(1),pp.1177 |
Papers・Author | Akaike Takaaki, Ida Tomoaki, Wei Fan-Yan, Nishida Motohiro, Kumagai Yoshito, Alam Md Morshedul, Ihara Hideshi, Sawa Tomohiro, Matsunaga Tetsuro, Kasamatsu Shingo, Nishimura Akiyuki, Morita Masanobu, Tomizawa Kazuhito, Nishimura Akira, Watanabe Satoshi, Inaba Kenji, Shima Hiroshi, Tanuma Nobuhiro, Jung Minkyung, Fujii Shigemoto, Watanabe Yasuo, Ohmuraya Masaki, Nagy Péter, Feelisch Martin, Fukuto Jon M, Motohashi Hozumi |
Publication date | 2017/10 |
Papers・Description | 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 Escherichia coli 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 L-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. |
DOI | 10.1038/s41467-017-01311-y |
PMID | 29079736 |