Ryuta Tobe1, Hisaaki Mihara2. 1. Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan. 2. Department of Biotechnology, College of Life Sciences, Ritsumeikan University, Kusatsu, Shiga 525-8577, Japan. Electronic address: mihara@fc.ritsumei.ac.jp.
Abstract
BACKGROUND: Selenophosphate, the key selenium donor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H2O. Although free selenide can be used as the in vitro selenium substrate for selenophosphate synthesis, the precise physiological system that donates in vivo selenium substrate to SPS has not yet been characterized completely. SCOPE OF REVIEW: In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. MAJOR CONCLUSIONS: Glutathione, selenocysteine lyase, cysteine desulfurase, and selenium-binding proteins are the candidates of selenium delivery system to SPS. The thioredoxin system is also implicated in the selenium delivery to SPS in Escherichia coli. GENERAL SIGNIFICANCE: Selenium delivered via a protein-bound selenopersulfide intermediate emerges as a central element not only in achieving specific selenoprotein biosynthesis but also in preventing the occurrence of toxic free selenide in the cell. This article is part of a Special Issue entitled "Selenium research in biochemistry and biophysics - 200 year anniversary".
BACKGROUND:Selenophosphate, the key seleniumdonor for the synthesis of selenoprotein and selenium-modified tRNA, is produced by selenophosphate synthetase (SPS) from ATP, selenide, and H2O. Although free selenide can be used as the in vitro selenium substrate for selenophosphate synthesis, the precise physiological system that donates in vivo selenium substrate to SPS has not yet been characterized completely. SCOPE OF REVIEW: In this review, we discuss selenium metabolism with respect to the delivery of selenium to SPS in selenoprotein biosynthesis. MAJOR CONCLUSIONS:Glutathione, selenocysteine lyase, cysteine desulfurase, and selenium-binding proteins are the candidates of selenium delivery system to SPS. The thioredoxin system is also implicated in the selenium delivery to SPS in Escherichia coli. GENERAL SIGNIFICANCE: Selenium delivered via a protein-bound selenopersulfide intermediate emerges as a central element not only in achieving specific selenoprotein biosynthesis but also in preventing the occurrence of toxic free selenide in the cell. This article is part of a Special Issue entitled "Selenium research in biochemistry and biophysics - 200 year anniversary".
Authors: Ligia M Watanabe; Ann C Hashimoto; Daniel J Torres; Marla J Berry; Lucia A Seale Journal: J Trace Elem Med Biol Date: 2020-07-11 Impact factor: 3.849
Authors: Alexey A Tinkov; Olga P Ajsuvakova; Tommaso Filippini; Ji-Chang Zhou; Xin Gen Lei; Eugenia R Gatiatulina; Bernhard Michalke; Margarita G Skalnaya; Marco Vinceti; Michael Aschner; Anatoly V Skalny Journal: Biomolecules Date: 2020-04-24
Authors: Lucia A Seale; Vedbar S Khadka; Mark Menor; Guoxiang Xie; Ligia M Watanabe; Alexandru Sasuclark; Kyrillos Guirguis; Herena Y Ha; Ann C Hashimoto; Karolina Peplowska; Maarit Tiirikainen; Wei Jia; Marla J Berry; Youping Deng Journal: Nutrients Date: 2019-10-26 Impact factor: 5.717
Authors: Marco Túlio Alves da Silva; Ivan Rosa E Silva; Lívia Maria Faim; Natália Karla Bellini; Murilo Leão Pereira; Ana Laura Lima; Teresa Cristina Leandro de Jesus; Fernanda Cristina Costa; Tatiana Faria Watanabe; Humberto D'Muniz Pereira; Sandro Roberto Valentini; Cleslei Fernando Zanelli; Júlio Cesar Borges; Marcio Vinicius Bertacine Dias; Júlia Pinheiro Chagas da Cunha; Bidyottam Mittra; Norma W Andrews; Otavio Henrique Thiemann Journal: PLoS Negl Trop Dis Date: 2020-10-05