ArticleThe Journal of biological chemistry2012
Selenocysteine insertion sequence (SECIS)-binding protein 2 alters conformational dynamics of residues involved in tRNA accommodation in 80 S ribosomes.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 23 citations in OpenAlex.
- Identification of a novel endogenous long non-coding RNA that inhibits selenoprotein P translation.Nucleic acids research · 2021Article
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- Modeling and gene knockdown to assess the contribution of nonsense-mediated decay, premature termination, and selenocysteine insertion to the selenoprotein hierarchy.RNA (New York, N.Y.) · 2016Article
- Chemical footprinting reveals conformational changes of 18S and 28S rRNAs at different steps of translation termination on the human ribosome.RNA (New York, N.Y.) · 2016Article
- 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
- Emergence and evolution.Topics in current chemistry · 2014Review
- The molecular biology of selenocysteine.Biomolecular concepts · 2013Review
- A novel insight into the mechanism of mammalian selenoprotein synthesis.RNA (New York, N.Y.) · 2013Article
- Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.Journal of molecular biology · 2013Article
- Identification of nucleotides and amino acids that mediate the interaction between ribosomal protein L30 and the SECIS element.BMC molecular biology · 2013Article
- Synthesis and decoding of selenocysteine and human health.Croatian medical journal · 2012Review
- The selenocysteine-specific elongation factor contains a novel and multi-functional domain.The Journal of biological chemistry · 2012Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Sec-tRNA(Sec) is site-specifically delivered at defined UGA codons in selenoprotein mRNAs. This recoding event is specified by the selenocysteine insertion sequence (SECIS) element and requires the selenocysteine (Sec)-specific elongation factor, eEFSec, and the SECIS binding protein, SBP2. Sec-tRNA(Sec) is delivered to the ribosome by eEFSec-GTP, but this ternary complex is not sufficient for Sec incorporation, indicating that its access to the ribosomal A-site is regulated. SBP2 stably associates with ribosomes, and mutagenic analysis indicates that this interaction is essential for Sec incorporation. However, the ribosomal function of SBP2 has not been elucidated. To shed light on the functional relevance of the SBP2-ribosome interaction, we screened the functional centers of the 28 S rRNA in translationally competent 80 S ribosomes using selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE). We demonstrate that SBP2 specifically alters the reactivity of specific residues in Helix 89 (H89) and expansion segment 31 (ES31). These results are indicative of a conformational change in response to SBP2 binding. Based on the known functions of H89 during translation, we propose that SBP2 allows Sec incorporation by either promoting Sec-tRNA(Sec) accommodation into the peptidyltransferase center and/or by stimulating the ribosome-dependent GTPase activity of eEFSec.
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Registered trials
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.