Journal ArticleDOI
Knowing when not to stop: selenocysteine incorporation in eukaryotes.
Susan C. Low,Marla J. Berry +1 more
TLDR
The regulation of translation frequently involves protein-RNA interactions, and in prokaryotes a single RNA-binding protein, a selenocysteine-specific elongation factor, interacts with both the tRNA and mRNA to confer decoding.About:
This article is published in Trends in Biochemical Sciences.The article was published on 1996-06-01. It has received 434 citations till now. The article focuses on the topics: Selenocysteine incorporation & Selenocysteine.read more
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Reactive oxygen species, antioxidants, and the mammalian thioredoxin system.
Jonas Nordberg,Elias S.J. Arnér +1 more
TL;DR: The TrxR-catalyzed regeneration of several antioxidant compounds, including ascorbic acid (vitamin C), selenium-containing substances, lipoic acid, and ubiquinone are summarized.
Journal ArticleDOI
Characterization of Mammalian Selenoproteomes
Gregory V. Kryukov,Sergi Castellano,Sergey V. Novoselov,Sergey V. Novoselov,Alexey V. Lobanov,Alexey V. Lobanov,Omid Zehtab,Omid Zehtab,Roderic Guigó,Roderic Guigó,Vadim N. Gladyshev,Vadim N. Gladyshev +11 more
TL;DR: This work identified selenoprotein genes in sequenced mammalian genomes by methods that rely on identification of selenocysteine insertion RNA structures, the coding potential of UGA codons, and the presence of cysteine-containing homologs.
Journal ArticleDOI
Biochemistry, cellular and molecular biology, and physiological roles of the iodothyronine selenodeiodinases.
TL;DR: The goal of this review is to place the exciting advances that have occurred in understanding of the molecular biology of the types 1, 2, and 3 (D1, D2, and D3, respectively) iodothyronine deiodinases into a biochemical and physiological context.
Journal ArticleDOI
Initiation of translation in prokaryotes and eukaryotes.
TL;DR: The binding of Met-tRNA to ribosomes is mediated by a GTP-binding protein in both prokaryotes and eukaryotes, but the more complex structure of the eukARYotic factor (eIF-2) and its association with other proteins underlie some aspects of initiation unique to eUKaryotes.
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Tissue-specific functions of individual glutathione peroxidases.
TL;DR: All individual isoenzymes are efficient peroxidases in principle, but beyond their mere antioxidant potential may exert cell- and tissue-specific roles in metabolic regulation, as is evident for PHGPx and may be expected for others.
References
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Type I iodothyronine deiodinase is a selenocysteine-containing enzyme
TL;DR: It is found that the mRNA for this enzyme contains a UGA codon for selenocysteine which is necessary for maximal enzyme activity and explains why conversion of T4 to T3 is impaired in experimental selenium deficiency2–6 and identifies an essential role for this trace element in thyroid hormone action.
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Selenocysteine: the 21st amino acid.
August Böck,Karl Forchhammer,Johann Heider,Walfred Leinfelder,Gary Sawers,B. Veprek,F. Zinoni +6 more
TL;DR: The aim of this article is to review the events leading to the elucidation of selenocysteine as being the 21st amino acid.
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Recognition of UGA as a selenocysteine codon in type I deiodinase requires sequences in the 3' untranslated region.
TL;DR: It is shown that successful incorporation of seleno-cysteine into this enzyme requires a specific 3′ untranslated (3′ut) segment of about 200 nucleotides, which is found in both rat and human 5′DI messenger RNAs.
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Evidence for specific selenium target tissues and new biologically important selenoproteins
TL;DR: With inadequate selenium intake there was a priority supply of the element to the brain, the reproductive and the endocrine organs, and at a molecular level to Se-containing proteins other than glutathione peroxidase.
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Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons.
TL;DR: The presence of SECIS elements in eukaryotic selenoprotein mRNAs permits complete flexibility in UGA codon position.