ArticleBMC evolutionary biology2009
Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins.
Article in BMC evolutionary biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 45 citations in OpenAlex.
- Genetics of selenoproteins and selenoprotein metabolism - An overview of current concepts and emerging aspects.Redox biology · 2026Review
- Sbp2l contributes to oligodendrocyte maturation through translational control in Tcf7l2 signaling.iScience · 2023Article
- Differential co-expression network analysis elucidated genes associated with sensitivity to farnesyltransferase inhibitor and prognosis of acute myeloid leukemia.Cancer medicine · 2023Article
- High-Resolution Ribosome Profiling Reveals Gene-Specific Details of UGA Re-Coding in Selenoprotein Biosynthesis.Biomolecules · 2022Article
- SECISBP2L-Mediated Selenoprotein Synthesis Is Essential for Autonomous Regulation of Oligodendrocyte Differentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- The expression of essential selenoproteins during development requires SECIS-binding protein 2-like.Life science alliance · 2022Article
- Article
- Identification of Survival-Specific Genes in Clear Cell Renal Cell Carcinoma Using a Customized Next-Generation Sequencing Gene Panel.Journal of personalized medicine · 2022Article
- Pathogenic Variants in Selenoproteins and Selenocysteine Biosynthesis Machinery.International journal of molecular sciences · 2021Review
- RNA-Associated Co-expression Network Identifies Novel Biomarkers for Digestive System Cancer.Frontiers in genetics · 2021Article
- Selenium-Dependent Read Through of the Conserved 3'-Terminal UGA Stop Codon of HIV-1 nef.American journal of biopharmacy and pharmaceutical sciences · 2021Article
- Tolerance to Selenoprotein Loss Differs between Human and Mouse.Molecular biology and evolution · 2020Article
- Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs.Journal of molecular biology · 2019Article
- The RNA-binding protein Secisbp2 differentially modulates UGA codon reassignment and RNA decay.Nucleic acids research · 2017Article
- Lokiarchaeota Marks the Transition between the Archaeal and Eukaryotic Selenocysteine Encoding Systems.Molecular biology and evolution · 2016Article
- Genome sequence of the organohalide-respiring Dehalogenimonas alkenigignens type strain (IP3-3(T)).Standards in genomic sciences · 2016Article
- The evolutionary and functional diversity of classical and lesser-known cytoplasmic and organellar translational GTPases across the tree of life.BMC genomics · 2015Article
- Secisbp2 is essential for embryonic development and enhances selenoprotein expression.Antioxidants & redox signaling · 2014Article
- Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage.RNA (New York, N.Y.) · 2014Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
backgroundThe co-translational incorporation of selenocysteine into nascent polypeptides by recoding the UGA stop codon occurs in all domains of life. In eukaryotes, this event requires at least three specific factors: SECIS binding protein 2 (SBP2), a specific translation elongation factor (eEFSec), selenocysteinyl tRNA, and a cis-acting selenocysteine insertion sequence (SECIS) element in selenoprotein mRNAs. While the phylogenetic relationships of selenoprotein families and the evolution of selenocysteine usage are well documented, the evolutionary history of SECIS binding proteins has not been explored.
resultsIn this report we present a phylogeny of the eukaryotic SECIS binding protein family which includes SBP2 and a related protein we herein term SBP2L. Here we show that SBP2L is an SBP2 paralogue in vertebrates and is the only form of SECIS binding protein in invertebrate deuterostomes, suggesting a key role in Sec incorporation in these organisms, but an SBP2/SBP2L fusion protein is unable to support Sec incorporation in vitro. An in-depth phylogenetic analysis of the conserved L7Ae RNA binding domain suggests an ancestral relationship with ribosomal protein L30. In addition, we describe the emergence of a motif upstream of the SBP2 RNA binding domain that shares significant similarity with a motif within the pseudouridine synthase Cbf5.
conclusionOur analysis suggests that SECIS binding proteins arose once in evolution but diverged significantly in multiple lineages. In addition, likely due to a gene duplication event in the early vertebrate lineage, SBP2 and SBP2L are paralogous in vertebrates.
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