ArticleNucleic acids research2007
An improved definition of the RNA-binding specificity of SECIS-binding protein 2, an essential component of the selenocysteine incorporation machinery.
Article in Nucleic acids research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 31 citations in OpenAlex.
- Running a genetic stop sign accelerates oxygen metabolism and energy production in horses.Science (New York, N.Y.) · 2025Article
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Methylation guide RNA evolution in archaea: structure, function and genomic organization of 110 C/D box sRNA families across six Pyrobaculum species.Nucleic acids research · 2018Article
- SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation.Nucleic acids research · 2017Article
- 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
- Hypermethylated-capped selenoprotein mRNAs in mammals.Nucleic acids research · 2014Article
- Selenoproteins: molecular pathways and physiological roles.Physiological reviews · 2014Review
- 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
- The selenocysteine-specific elongation factor contains a novel and multi-functional domain.The Journal of biological chemistry · 2012Article
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- Crystallization and preliminary X-ray structure analysis of human ribosomal protein L30e.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Signature amino acids enable the archaeal L7Ae box C/D RNP core protein to recognize and bind the K-loop RNA motif.RNA (New York, N.Y.) · 2010Article
- Evolutionary history of selenocysteine incorporation from the perspective of SECIS binding proteins.BMC evolutionary biology · 2009Article
- Novel structural determinants in human SECIS elements modulate the translational recoding of UGA as selenocysteine.Nucleic acids research · 2009Article
- A short motif in Drosophila SECIS Binding Protein 2 provides differential binding affinity to SECIS RNA hairpins.Nucleic acids research · 2009Article
- SECISaln, a web-based tool for the creation of structure-based alignments of eukaryotic SECIS elements.Bioinformatics (Oxford, England) · 2009Article
- A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.The Journal of biological chemistry · 2008Article
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Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
By binding to SECIS elements located in the 3'-UTR of selenoprotein mRNAs, the protein SBP2 plays a key role in the assembly of the selenocysteine incorporation machinery. SBP2 contains an L7Ae/L30 RNA-binding domain similar to that of protein 15.5K/Snu13p, which binds K-turn motifs with a 3-nt bulge loop closed by a tandem of G.A and A.G pairs. Here, by SELEX experiments, we demonstrate the capacity of SBP2 to bind such K-turn motifs with a protruding U residue. However, we show that conversion of the bulge loop into an internal loop reinforces SBP2 affinity and to a greater extent RNP stability. Opposite variations were found for Snu13p. Accordingly, footprinting assays revealed strong contacts of SBP2 with helices I and II and the 5'-strand of the internal loop, as opposed to the loose interaction of Snu13p. Our data also identifies new determinants for SBP2 binding which are located in helix II. Among the L7Ae/L30 family members, these determinants are unique to SBP2. Finally, in accordance with functional data on SECIS elements, the identity of residues at positions 2 and 3 in the loop influences SBP2 affinity. Altogether, the data provide a very precise definition of the SBP2 RNA specificity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.