ArticleThe Journal of biological chemistry2012
The selenocysteine-specific elongation factor contains a novel and multi-functional domain.
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 18 papers.
What it found
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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.
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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.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Selenium in the Preterm Infant: Are We Supplementing Enough in This Vulnerable Population?Nutrients · 2026Review
- Systematic Analysis of Genes Related to Selenium Bioaccumulation in Microalgae: A Review.Biology · 2023Review
- SECISBP2L-Mediated Selenoprotein Synthesis Is Essential for Autonomous Regulation of Oligodendrocyte Differentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon.Science (New York, N.Y.) · 2022Article
- Mechanisms Affecting the Biosynthesis and Incorporation Rate of Selenocysteine.Molecules (Basel, Switzerland) · 2021Review
- 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
- SECIS-binding protein 2 interacts with the SMN complex and the methylosome for selenoprotein mRNP assembly and translation.Nucleic acids research · 2017Article
- Crystal structures of the human elongation factor eEFSec suggest a non-canonical mechanism for selenocysteine incorporation.Nature communications · 2016Article
- 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
- Article
- Structural asymmetry of the terminal catalytic complex in selenocysteine synthesis.The Journal of biological chemistry · 2014Article
- Regulation of selenocysteine incorporation into the selenium transport protein, selenoprotein P.The Journal of biological chemistry · 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
- 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
- Synthesis and decoding of selenocysteine and human health.Croatian medical journal · 2012Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The selenocysteine (Sec)-specific eukaryotic elongation factor (eEFSec) delivers the aminoacylated selenocysteine-tRNA (Sec-tRNA(Sec)) to the ribosome and suppresses UGA codons that are upstream of Sec insertion sequence (SECIS) elements bound by SECIS-binding protein 2 (SBP2). Multiple studies have highlighted the importance of SBP2 forming a complex with the SECIS element, but it is not clear how this regulates eEFSec during Sec incorporation. Compared with the canonical elongation factor eEF1A, eEFSec has a unique C-terminal extension called Domain IV. To understand the role of Domain IV in Sec incorporation, we examined a series of mutant proteins for all of the known molecular functions for eEFSec: GTP hydrolysis, Sec-tRNA(Sec) binding, and SBP2/SECIS binding. In addition, wild-type and mutant versions of eEFSec were analyzed for Sec incorporation activity in a novel eEFSec-dependent translation extract. We have found that Domain IV is essential for both tRNA and SBP2 binding as well as regulating GTPase activity. We propose a model where the SBP2/SECIS complex activates eEFSec by directing functional interactions between Domain IV and the ribosome to promote Sec-tRNA(Sec) binding and accommodation into the ribosomal A-site.
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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.