Thioredoxin Reductase 1 Is Important for Selenoprotein Biosynthesis in HeLa Cells

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  • Kurokawa Suguru
    Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University
  • Mihara Hisaaki
    Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University
  • Yokoyama Izumi
    Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University
  • Mochizuki Michika
    Department of Biological Responses, Institute for Virus Research, Kyoto University
  • Yodoi Junji
    Department of Biological Responses, Institute for Virus Research, Kyoto University
  • Tamura Takashi
    Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University
  • Kurihara Tatsuo
    Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University
  • Esaki Nobuyoshi
    Laboratory of Molecular Microbial Science, Institute for Chemical Research, Kyoto University

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Abstract

Selenium, an essential trace element, is co-translationally incorporated into selenoproteins as the 21st amino acid selenocysteine. Selenite serves as an inorganic selenium source for selenoprotein biosynthesis through reduction to selenide, which is converted to selenophosphate, the essential selenium donor in selenocysteyl-tRNA[Ser]Sec synthesis. However, the pathways for selenite reduction in mammalian cells have not yet been clarified. Based on metabolic labeling with [75Se]selenite and RNA silencing studies, we here present evidence that thioredoxin reductase 1, but not thioredoxin, is crucial for selenite utilization to form selenoproteins in HeLa cells. We suggest that thioredoxin reductase 1 plays a role as a selenite-reducing enzyme in vivo.

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