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The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element

Selenocysteine insertion into selenoproteins involves the translational recoding of UGA stop codons. In mammals, selenoprotein expression further depends on selenium availability, which has been particularly described for glutathione peroxidase 1 and 4 (Gpx1 and Gpx4). The SECIS element located in t...

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Published in:RNA biology 2012-05, Vol.9 (5), p.681-690
Main Authors: Latrèche, Lynda, Duhieu, Stéphane, Touat-Hamici, Zahia, Jean-Jean, Olivier, Chavatte, Laurent
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cited_by cdi_FETCH-LOGICAL-c559t-fcb4ed05be29547f3d7006a3fa3a945713b1eb5570e875dd8cff487154df72743
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creator Latrèche, Lynda
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description Selenocysteine insertion into selenoproteins involves the translational recoding of UGA stop codons. In mammals, selenoprotein expression further depends on selenium availability, which has been particularly described for glutathione peroxidase 1 and 4 (Gpx1 and Gpx4). The SECIS element located in the 3′UTR of the selenoprotein mRNAs is a modulator of UGA recoding efficiency in adequate selenium conditions. One of the current models for the UGA recoding mechanism proposes that the SECIS binds SECIS-binding protein 2 (SBP2), which then recruits a selenocysteine-specific elongation factor (EFsec) and tRNA Sec to the ribosome, where L30 acts as an anchor. The involvement of the SECIS in modulation of UGA recoding activity was investigated, together with SBP2 and EFsec, in Hek293 cells cultured with various selenium levels. Luciferase reporter constructs, in transiently or stably expressing cell lines, were used to analyze the differential expression of Gpx1 and Gpx4. We showed that, upon selenium fluctuation, the modulation of UGA recoding efficiency depends on the nature of the SECIS, with Gpx1 being more sensitive than Gpx4. Attenuation of SBP2 and EFsec levels by shRNAs confirmed that both factors are essential for efficient selenocysteine insertion. Strikingly, in a context of either EFsec or SBP2 attenuation, the decrease in UGA recoding efficiency is dependent on the nature of the SECIS, GPx1 being more sensitive. Finally, the profusion of selenium of the culture medium exacerbates the lack of factors involved in selenocysteine insertion.
doi_str_mv 10.4161/rna.20147
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ispartof RNA biology, 2012-05, Vol.9 (5), p.681-690
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1555-8584
language eng
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source PubMed Central Free
subjects 3' Untranslated Regions
Animals
Base Sequence
Binding
Biology
Bioscience
Calcium
Cancer
Cell
Cellular Biology
Codon, Terminator - genetics
Cycle
EFsec
Gene Expression Regulation, Enzymologic
glutathione peroxidase
Glutathione Peroxidase - genetics
Glutathione Peroxidase - metabolism
HEK293 Cells
Humans
Inverted Repeat Sequences
Landes
Life Sciences
Molecular Sequence Data
Nucleic Acid Conformation
Organogenesis
Peptide Elongation Factors - genetics
Peptide Elongation Factors - metabolism
Protein Biosynthesis
Proteins
Rats
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
SBP2
SECIS
selenium
Selenium - physiology
selenoprotein
UGA recoding
title The differential expression of glutathione peroxidase 1 and 4 depends on the nature of the SECIS element
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