ArticleRNA (New York, N.Y.)2013
A novel insight into the mechanism of mammalian selenoprotein synthesis.
Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.Structure (London, England : 1993) · 2024Article
- On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins.Biochimica et biophysica acta. General subjects · 2018Review
- Complementary-addressed site-directed spin labeling of long natural RNAs.Nucleic acids research · 2016Article
- Hydroxylation and translational adaptation to stress: some answers lie beyond the STOP codon.Cellular and molecular life sciences : CMLS · 2016Review
- 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
- antaRNA: ant colony-based RNA sequence design.Bioinformatics (Oxford, England) · 2015Article
- Association analysis of selenoprotein S polymorphisms in Chinese Han with susceptibility to gastric cancer.International journal of clinical and experimental medicine · 2015Article
- 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
- SelenoDB 2.0: annotation of selenoprotein genes in animals and their genetic diversity in humans.Nucleic acids research · 2014Article
- General approach for introduction of various chemical labels in specific RNA locations based on insertion of amino linkers.Molecules (Basel, Switzerland) · 2013Review
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amino acid selenocysteine is encoded by UGA, usually a stop codon, thus requiring a specialized machinery to enable its incorporation into selenoproteins. The machinery comprises the tRNA(Sec), a 3'-UTR mRNA stem-loop termed SElenoCysteine Insertion Sequence (SECIS), which is mandatory for recoding UGA as a Sec codon, the SECIS Binding Protein 2 (SBP2), and other proteins. Little is known about the molecular mechanism and, in particular, when, where, and how the SECIS and SBP2 contact the ribosome. Previous work by others used the isolated SECIS RNA to address this question. Here, we developed a novel approach using instead engineered minimal selenoprotein mRNAs containing SECIS elements derivatized with photoreactive groups. By cross-linking experiments in rabbit reticulocyte lysate, new information could be gained about the SBP2 and SECIS contacts with components of the translation machinery at various translation steps. In particular, we found that SBP2 was bound only to the SECIS in 48S pre-initiation and 80S pretranslocation complexes. In the complex where the Sec-tRNA(Sec) was accommodated to the A site but transpeptidation was blocked, SBP2 bound the ribosome and possibly the SECIS element as well, and the SECIS had flexible contacts with the 60S ribosomal subunit involving several ribosomal proteins. Altogether, our findings led to broadening our understanding about the unique mechanism of selenocysteine incorporation in mammals.
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