Evidence map›Paper›PMID 29069514›Full record

ArticleNucleic acids research2017

Multiple RNA structures affect translation initiation and UGA redefinition efficiency during synthesis of selenoprotein P.

Marco Mariotti, Sumangala Shetty, Lisa Baird, Sen Wu, Gary Loughran, Paul R Copeland, John F Atkins, Michael T Howard

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Ribosome Fate during Decoding of UGA-Sec Codons.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Bioinformatics of Selenoproteins.Antioxidants & redox signaling · 2020
    Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Molecular mechanism of selenoprotein P synthesis.Biochimica et biophysica acta. General subjects · 2018
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 6 institutions in 3 countries.

Marco MariottiDivision of Genetics, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, Boston, MA USA.
Sumangala ShettyDepartment of Biochemistry and Molecular Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, NJ USA.
Lisa BairdDepartment of Human Genetics, University of Utah, Salt Lake City, UT, USA.
Sen WuState Key Laboratory of Agrobiotechnology, China Agricultural University, Beijing 100193, People's Republic of China.
Gary LoughranBiochemistry and Cell Biology, University College Cork, Cork, Ireland.
Paul R CopelandDepartment of Biochemistry and Molecular Biology, Rutgers Robert Wood Johnson Medical School, Piscataway, NJ USA.
John F AtkinsDepartment of Human Genetics, University of Utah, Salt Lake City, UT, USA.
Michael T HowardDepartment of Human Genetics, University of Utah, Salt Lake City, UT, USA.
University of Utah · USChina Agricultural University · CNHarvard University · USJohnson University · USRutgers, The State University of New Jersey · USUniversity College Cork · IE

Funding

The effects of dietary selenium on translational control of protein synthesisR01GM114291 · NIGMS · UNIVERSITY OF UTAH · PI HOWARD, MICHAEL T · 2015 to 2022
$2.4M
NIGMS NIH HHS R01 GM114291
6 · The paper itself

Abstract

Gene-specific expansion of the genetic code allows for UGA codons to specify the amino acid selenocysteine (Sec). A striking example of UGA redefinition occurs during translation of the mRNA coding for the selenium transport protein, selenoprotein P (SELENOP), which in vertebrates may contain up to 22 in-frame UGA codons. Sec incorporation at the first and downstream UGA codons occurs with variable efficiencies to control synthesis of full-length and truncated SELENOP isoforms. To address how the Selenop mRNA can direct dynamic codon redefinition in different regions of the same mRNA, we undertook a comprehensive search for phylogenetically conserved RNA structures and examined the function of these structures using cell-based assays, in vitro translation systems, and in vivo ribosome profiling of liver tissue from mice carrying genomic deletions of 3' UTR selenocysteine-insertion-sequences (SECIS1 and SECIS2). The data support a novel RNA structure near the start codon that impacts translation initiation, structures located adjacent to UGA codons, additional coding sequence regions necessary for efficient production of full-length SELENOP, and distinct roles for SECIS1 and SECIS2 at UGA codons. Our results uncover a remarkable diversity of RNA elements conducting multiple occurrences of UGA redefinition to control the synthesis of full-length and truncated SELENOP isoforms.

Indexed as

Peptide Chain Initiation, Translational3' Untranslated RegionsAnimalsBase SequenceCodon, InitiatorCodon, TerminatorHumansMice, Inbred C57BLNucleic Acid ConformationProtein IsoformsRibosomesRNA, MessengerSelenocysteineSelenoprotein PSequence Homology, Nucleic Acid3' Untranslated RegionsCodon, InitiatorCodon, TerminatorProtein IsoformsRNA, MessengerSelenocysteineSelenoprotein P

Identifiers

PMID29069514
PMCPMC5727441
OpenAlexW2766709260

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

None linked

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.