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Molecular Research of Selenocysteine in Selenoproteins

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Biochemistry".

Deadline for manuscript submissions: 20 October 2024 | Viewed by 4639

Special Issue Editor


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Guest Editor
Department of Biochemistry and Molecular Biology, University of Georgia, Athens, GA 30602, USA
Interests: genetic code expansion; selenocysteine; system engineering; biophysics; synthetic biology

Special Issue Information

Dear Colleagues,

Selenium is an essential micronutrient for humans. Found primarily in the form of selenocysteine, the 21st naturally occurring amino acid, selenocysteine is incorporated into nascent selenoproteins at specified UGA codons through a sophisticated translation pathway developed by nature. These methods of biosynthesis and insertion of selenocysteine differ in all three domains of life. In humans, 25 identified selenoproteins have been linked to various diseases, including neurological, cardiovascular, reproductive, and infectious diseases, cancer, and diabetes. The pathologies of these diseases are associated with imbalances between the generation and elimination of reactive oxygen or nitrogen species. Selenoproteins are not unique to humans or eukaryotes, but play critical roles in bacterial physiology and archaeal methanogenesis. Various mouse and cell models and functional genomics, as well as advances in chemical, synthetic biology, and bioinformatics technologies, have significantly driven forward the field of selenium biology. This Special Issue welcomes submissions addressing any aspect of selenium and selenoproteins in any domain of life.

Dr. Natalie Krahn
Guest Editor

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Keywords

  • selenocysteine
  • selenoproteins
  • selenium
  • oxidoreductase
  • antioxidant
  • suppression

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Published Papers (4 papers)

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Research

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14 pages, 1549 KiB  
Article
Selenium Discrepancies in Fetal Bovine Serum: Impact on Cellular Selenoprotein Expression
by François Parant, Fabrice Mure, Julien Maurin, Léana Beauvilliers, Chaïma Chorfa, Chaymae El Jamali, Théophile Ohlmann and Laurent Chavatte
Int. J. Mol. Sci. 2024, 25(13), 7261; https://doi.org/10.3390/ijms25137261 - 1 Jul 2024
Cited by 1 | Viewed by 1013
Abstract
Selenium is an essential trace element in our diet, crucial for the composition of human selenoproteins, which include 25 genes such as glutathione peroxidases and thioredoxin reductases. The regulation of the selenoproteome primarily hinges on the bioavailability of selenium, either from dietary sources [...] Read more.
Selenium is an essential trace element in our diet, crucial for the composition of human selenoproteins, which include 25 genes such as glutathione peroxidases and thioredoxin reductases. The regulation of the selenoproteome primarily hinges on the bioavailability of selenium, either from dietary sources or cell culture media. This selenium-dependent control follows a specific hierarchy, with “housekeeping” selenoproteins maintaining constant expression while “stress-regulated” counterparts respond to selenium level fluctuations. This study investigates the variability in fetal bovine serum (FBS) selenium concentrations among commercial batches and its effects on the expression of specific stress-related cellular selenoproteins. Despite the limitations of our study, which exclusively used HEK293 cells and focused on a subset of selenoproteins, our findings highlight the substantial impact of serum selenium levels on selenoprotein expression, particularly for GPX1 and GPX4. The luciferase reporter assay emerged as a sensitive and precise method for evaluating selenium levels in cell culture environments. While not exhaustive, this analysis provides valuable insights into selenium-mediated selenoprotein regulation, emphasizing the importance of serum composition in cellular responses and offering guidance for researchers in the selenoprotein field. Full article
(This article belongs to the Special Issue Molecular Research of Selenocysteine in Selenoproteins)
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24 pages, 2289 KiB  
Article
Transcriptomic Changes in Response to Form of Selenium on the Interferon-Tau Signaling Mechanism in the Caruncular Tissue of Beef Heifers at Maternal Recognition of Pregnancy
by Sarah N. Carr, Benjamin R. Crites, Harshraj Shinde and Phillip J. Bridges
Int. J. Mol. Sci. 2023, 24(24), 17327; https://doi.org/10.3390/ijms242417327 - 10 Dec 2023
Cited by 2 | Viewed by 1297
Abstract
We have reported that selenium (Se) provided to grazing beef cattle in an inorganic (ISe) form versus a 1:1 mixture (MIX) of inorganic and organic (OSe) forms affects cholesterol biosynthesis in the corpus luteum (CL), the abundance of interferon tau (IFNτ) and progesterone [...] Read more.
We have reported that selenium (Se) provided to grazing beef cattle in an inorganic (ISe) form versus a 1:1 mixture (MIX) of inorganic and organic (OSe) forms affects cholesterol biosynthesis in the corpus luteum (CL), the abundance of interferon tau (IFNτ) and progesterone (P4)-induced mRNAs in the caruncular (CAR) tissue of the endometrium, and conceptus length at maternal recognition of pregnancy (MRP). In this study, beef heifers were supplemented with a vitamin–mineral mix containing 35 ppm Se as ISe or MIX to achieve a Se-adequate status. Inseminated heifers were killed at MRP (d 17, n = 6 per treatment) for tissue collection. In CAR samples from MIX versus ISe heifers, qPCR revealed that mRNA encoding the thyroid regulating DIO2 and DIO3 was decreased (p < 0.05) and a complete transcriptomic analysis revealed effects on the interferon JAK-STAT1/2 pathway, including decreased expression of mRNAs encoding the classical interferon stimulated genes IFIT1, IFIT2, IFIT3, IRF1, IRF9, ISG15, OAS2, and RSAD2 (p < 0.05). Treatment also affected the abundance of mRNAs contributing to the immunotolerant environment (p < 0.05). In combination, these findings suggest more advanced preparation of the CAR and developing conceptus for implantation and to evade immune rejection by the maternal system in MIX- vs. ISe-treated heifers. Full article
(This article belongs to the Special Issue Molecular Research of Selenocysteine in Selenoproteins)
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Review

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18 pages, 3012 KiB  
Review
Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins
by Antavius Cain and Natalie Krahn
Int. J. Mol. Sci. 2024, 25(18), 10101; https://doi.org/10.3390/ijms251810101 - 20 Sep 2024
Viewed by 449
Abstract
Selenocysteine (Sec) is an essential amino acid that distinguishes itself from cysteine by a selenium atom in place of a sulfur atom. This single change imparts distinct chemical properties to Sec which are crucial for selenoprotein (Sec-containing protein) function. These properties include a [...] Read more.
Selenocysteine (Sec) is an essential amino acid that distinguishes itself from cysteine by a selenium atom in place of a sulfur atom. This single change imparts distinct chemical properties to Sec which are crucial for selenoprotein (Sec-containing protein) function. These properties include a lower pKa, enhanced nucleophilicity, and reversible oxidation. However, studying Sec incorporation in proteins is a complex process. While we find Sec in all domains of life, each domain has distinct translation mechanisms. These mechanisms are unique to canonical translation and are composed of Sec-specific enzymes and an mRNA hairpin to drive recoding of the UGA stop codon with Sec. In this review, we highlight the obstacles that arise when investigating Sec insertion, and the role that Sec has in proteins. We discuss the strategic methods implemented in this field to address these challenges. Though the Sec translation system is complex, a remarkable amount of information has been obtained and specialized tools have been developed. Continued studies in this area will provide a deeper understanding on the role of Sec in the context of proteins, and the necessity that we have for maintaining this complex translation machinery to make selenoproteins. Full article
(This article belongs to the Special Issue Molecular Research of Selenocysteine in Selenoproteins)
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21 pages, 1127 KiB  
Review
Biosynthesis, Engineering, and Delivery of Selenoproteins
by David E. Wright and Patrick O’Donoghue
Int. J. Mol. Sci. 2024, 25(1), 223; https://doi.org/10.3390/ijms25010223 - 22 Dec 2023
Cited by 2 | Viewed by 1294
Abstract
Selenocysteine (Sec) was discovered as the 21st genetically encoded amino acid. In nature, site-directed incorporation of Sec into proteins requires specialized biosynthesis and recoding machinery that evolved distinctly in bacteria compared to archaea and eukaryotes. Many organisms, including higher plants and most fungi, [...] Read more.
Selenocysteine (Sec) was discovered as the 21st genetically encoded amino acid. In nature, site-directed incorporation of Sec into proteins requires specialized biosynthesis and recoding machinery that evolved distinctly in bacteria compared to archaea and eukaryotes. Many organisms, including higher plants and most fungi, lack the Sec-decoding trait. We review the discovery of Sec and its role in redox enzymes that are essential to human health and important targets in disease. We highlight recent genetic code expansion efforts to engineer site-directed incorporation of Sec in bacteria and yeast. We also review methods to produce selenoproteins with 21 or more amino acids and approaches to delivering recombinant selenoproteins to mammalian cells as new applications for selenoproteins in synthetic biology. Full article
(This article belongs to the Special Issue Molecular Research of Selenocysteine in Selenoproteins)
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