Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics

Takaaki Akaike (), Tomoaki Ida, Fan-Yan Wei, Motohiro Nishida, Yoshito Kumagai, Md. Morshedul Alam, Hideshi Ihara, Tomohiro Sawa, Tetsuro Matsunaga, Shingo Kasamatsu, Akiyuki Nishimura, Masanobu Morita, Kazuhito Tomizawa, Akira Nishimura, Satoshi Watanabe, Kenji Inaba, Hiroshi Shima, Nobuhiro Tanuma, Minkyung Jung, Shigemoto Fujii, Yasuo Watanabe, Masaki Ohmuraya, Péter Nagy, Martin Feelisch, Jon M. Fukuto and Hozumi Motohashi
Additional contact information
Takaaki Akaike: Tohoku University Graduate School of Medicine
Tomoaki Ida: Tohoku University Graduate School of Medicine
Fan-Yan Wei: Kumamoto University
Motohiro Nishida: National Institutes of Natural Sciences
Yoshito Kumagai: University of Tsukuba
Md. Morshedul Alam: Tohoku University
Hideshi Ihara: Osaka Prefecture University
Tomohiro Sawa: Kumamoto University
Tetsuro Matsunaga: Tohoku University Graduate School of Medicine
Shingo Kasamatsu: Tohoku University Graduate School of Medicine
Akiyuki Nishimura: National Institutes of Natural Sciences
Masanobu Morita: Tohoku University Graduate School of Medicine
Kazuhito Tomizawa: Kumamoto University
Akira Nishimura: Tohoku University Graduate School of Medicine
Satoshi Watanabe: Tohoku University
Kenji Inaba: Tohoku University
Hiroshi Shima: Miyagi Cancer Center Research Institute
Nobuhiro Tanuma: Miyagi Cancer Center Research Institute
Minkyung Jung: Tohoku University Graduate School of Medicine
Shigemoto Fujii: Tohoku University Graduate School of Medicine
Yasuo Watanabe: Showa Pharmaceutical University
Masaki Ohmuraya: Nishinomiya
Péter Nagy: National Institute of Oncology
Martin Feelisch: University of Southampton, Southampton General Hospital and Institute for Life Sciences
Jon M. Fukuto: Sonoma State University
Hozumi Motohashi: Tohoku University

Nature Communications, 2017, vol. 8, issue 1, 1-15

Abstract: Abstract 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.

Date: 2017
References: Add references at CitEc
Citations: View citations in EconPapers (5)

Downloads: (external link)
https://www.nature.com/articles/s41467-017-01311-y Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01311-y

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-017-01311-y

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().