Persulfide synthases that are functionally coupled with translation mediate sulfur respiration in mammalian cells

Shigemoto Fujii, Tomohiro Sawa, Hozumi Motohashi, Takaaki Akaike

Research output: Contribution to journalReview articlepeer-review

14 Citations (Scopus)

Abstract

Cysteine persulfide and polysulfide are produced in cells and exist in abundance in both low MW and protein fractions. However, the mechanism of regulation of the formation of cellular cysteine polysulfides and the physiological functions of cysteine persulfides/polysulfides produced in cells are not fully understood. We recently demonstrated that cysteinyl-tRNA synthetase (CARS) is a novel cysteine persulfide synthase. CARS is involved in protein polysulfidation that is coupled with translation. In particular, mitochondria function in biogenesis and bioenergetics is also supported and up-regulated by cysteine persulfide derived from mitochondrial CARS (also known as CARS2). Here, we provide an overview of recent advances in reactive persulfide research and our understanding of the mechanisms underlying the formation and the physiological roles of reactive persufides, with a primary focus on the formation of cysteine persulfide by CARS and the most fundamental mitochondrial bioenergetics mediated by persulfides, that is, sulfur respiration. Linked Articles: This article is part of a themed section on Chemical Biology of Reactive Sulfur Species. To view the other articles in this section visit http://onlinelibrary.wiley.com/doi/10.1111/bph.v176.4/issuetoc.

Original languageEnglish
Pages (from-to)607-615
Number of pages9
JournalBritish Journal of Pharmacology
Volume176
Issue number4
DOIs
Publication statusPublished - 2019 Feb
Externally publishedYes

ASJC Scopus subject areas

  • Pharmacology

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