ArticleJournal of molecular biology2013
Reconstitution of selenocysteine incorporation reveals intrinsic regulation by SECIS elements.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
23 citing papers in PubMed, 35 citations in OpenAlex.
- Selenoproteins: Minute yet vital players governing cellular fate.Genes & diseases · 2026Review
- Overcoming Challenges with Biochemical Studies of Selenocysteine and Selenoproteins.International journal of molecular sciences · 2024Review
- Engineering of enzymes using non-natural amino acids.Bioscience reports · 2022Review
- Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.Science (New York, N.Y.) · 2022Article
- The expression of essential selenoproteins during development requires SECIS-binding protein 2-like.Life science alliance · 2022Article
- Bioinformatics of Selenoproteins.Antioxidants & redox signaling · 2020Review
- Human Disorders Affecting the Selenocysteine Incorporation Pathway Cause Systemic Selenoprotein Deficiency.Antioxidants & redox signaling · 2020Article
- Processive Recoding and Metazoan Evolution of Selenoprotein P: Up to 132 UGAs in Molluscs.Journal of molecular biology · 2019Article
- New Directions for Understanding the Codon Redefinition Required for Selenocysteine Incorporation.Biological trace element research · 2019Review
- Concerted 2-5A-Mediated mRNA Decay and Transcription Reprogram Protein Synthesis in the dsRNA Response.Molecular cell · 2019Article
- Processive incorporation of multiple selenocysteine residues is driven by a novel feature of the selenocysteine insertion sequence.The Journal of biological chemistry · 2018Article
- The Selenium Transport Protein, Selenoprotein P, Requires Coding Sequence Determinants to Promote Efficient Selenocysteine Incorporation.Journal of molecular biology · 2018Article
- Molecular mechanism of selenoprotein P synthesis.Biochimica et biophysica acta. General subjects · 2018Review
- Recent advances in the optical control of protein function through genetic code expansion.Current opinion in chemical biology · 2018Review
- The RNA-binding protein Secisbp2 differentially modulates UGA codon reassignment and RNA decay.Nucleic acids research · 2017Article
- The utilization of selenocysteine-tRNATranslation (Austin, Tex.) · 2017Article
- Article
- A synthetic tRNA for EF-Tu mediated selenocysteine incorporation in vivo and in vitro.FEBS letters · 2015Article
- Article
- Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.The Journal of biological chemistry · 2014Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Selenoproteins are present in all three domains of life and are responsible for a major part of a cell's antioxidant defense against reactive oxygen species. Synthesis of selenoproteins requires the decoding of a UGA codon as selenocysteine (Sec) instead of translation termination. Sec is incorporated into the growing polypeptide chain during translation elongation and is known to require a set of highly specific factors: the Sec insertion sequence (SECIS) element in the 3' untranslated region, Sec-tRNA(Sec), the Sec-specific elongation factor eEFSec, and SECIS binding protein 2. Since reconstitution has not been reported, whether these factors are sufficient is unknown. Here, we report a novel in vitro translation system in which Sec incorporation has been reconstituted from purified components introduced into a Sec naive system. In addition, we developed a novel method to purify Sec-tRNA(Sec) and active eEFSec/GTP/tRNA ternary complex. We found that the known basal factors are sufficient for Sec incorporation in vitro. Using this highly manipulable system, we have also found that ribosomes from non-Sec-utilizing organisms cannot support Sec incorporation and that some SECIS elements are intrinsically less efficient than others. Having identified the essential set of factors, this work removes a significant barrier to our understanding of the mechanism of Sec incorporation.
Indexed as
Identifiers
What OpenQuestion holds
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.