ArticleNucleic acids research2009
A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins.
Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 44 citations in OpenAlex.
- rRNA expansion segment 7 in eukaryotes: from Signature Fold to tentacles.Nucleic acids research · 2022Article
- Human Genetic Disorders Resulting in Systemic Selenoprotein Deficiency.International journal of molecular sciences · 2021Review
- MeCP2: The Genetic Driver of Rett Syndrome Epigenetics.Frontiers in genetics · 2021Review
- Article
- Human Disorders Affecting the Selenocysteine Incorporation Pathway Cause Systemic Selenoprotein Deficiency.Antioxidants & redox signaling · 2020Article
- Ribosome profiling of selenoproteinsThe Journal of biological chemistry · 2019Article
- Selenium-sensitive miRNA-181a-5p targeting SBP2 regulates selenoproteins expression in cartilage.Journal of cellular and molecular medicine · 2018Article
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- The hsa-miR-181a-5p reduces oxidation resistance by controlling SECISBP2 in osteoarthritis.BMC musculoskeletal disorders · 2018Article
- Adjustments, extinction, and remains of selenocysteine incorporation machinery in the nematode lineage.RNA (New York, N.Y.) · 2014Article
- The SBP2 protein central to selenoprotein synthesis contacts the human ribosome at expansion segment 7L of the 28S rRNA.RNA (New York, N.Y.) · 2014Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- Hypermethylated-capped selenoprotein mRNAs in mammals.Nucleic acids research · 2014Article
- Characterization of the UGA-recoding and SECIS-binding activities of SECIS-binding protein 2.RNA biology · 2014Article
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
- A novel insight into the mechanism of mammalian selenoprotein synthesis.RNA (New York, N.Y.) · 2013Article
- Identification of nucleotides and amino acids that mediate the interaction between ribosomal protein L30 and the SECIS element.BMC molecular biology · 2013Article
- Article
- Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Analyses of fruit flies that do not express selenoproteins or express the mouse selenoprotein, methionine sulfoxide reductase B1, reveal a role of selenoproteins in stress resistance.The Journal of biological chemistry · 2011Article
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Authors and funding
8 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Selenoproteins contain the amino acid selenocysteine which is encoded by a UGA Sec codon. Recoding UGA Sec requires a complex mechanism, comprising the cis-acting SECIS RNA hairpin in the 3'UTR of selenoprotein mRNAs, and trans-acting factors. Among these, the SECIS Binding Protein 2 (SBP2) is central to the mechanism. SBP2 has been so far functionally characterized only in rats and humans. In this work, we report the characterization of the Drosophila melanogaster SBP2 (dSBP2). Despite its shorter length, it retained the same selenoprotein synthesis-promoting capabilities as the mammalian counterpart. However, a major difference resides in the SECIS recognition pattern: while human SBP2 (hSBP2) binds the distinct form 1 and 2 SECIS RNAs with similar affinities, dSBP2 exhibits high affinity toward form 2 only. In addition, we report the identification of a K (lysine)-rich domain in all SBP2s, essential for SECIS and 60S ribosomal subunit binding, differing from the well-characterized L7Ae RNA-binding domain. Swapping only five amino acids between dSBP2 and hSBP2 in the K-rich domain conferred reversed SECIS-binding properties to the proteins, thus unveiling an important sequence for form 1 binding.
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