Evidence map›Paper›PMID 18948268›Full record

ArticleThe Journal of biological chemistry2008

A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment.

Jesse Donovan, Kelvin Caban, Ruchira Ranaweera, Jonathan N Gonzalez-Flores, Paul R Copeland

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.4field-weighted citation impact, top 8% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Human Genetic Disorders Resulting in Systemic Selenoprotein Deficiency.International journal of molecular sciences · 2021
    Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Ribosome profiling of selenoproteinsThe Journal of biological chemistry · 2019
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

5 authors at 1 institution in 1 country.

Jesse DonovanDepartment of Molecular Genetics, Microbiology and Immunology, University of Medicine and Dentistry of New Jersey, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854, USA.
Kelvin Caban
Ruchira Ranaweera
Jonathan N Gonzalez-Flores
Paul R Copeland
Johnson University · US

Funding

Functional Analysis of SBP2 and Selenocysteine IncorporationR01GM077073 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI COPELAND, PAUL R · 2006 to 2022
$5.5M
VIRUS-HOST INTERACTIONS IN EUKARYOTIC CELLST32AI007403 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI BREWER, GARY A. · 1991 to 2014
$1.7M
The translational control of selenoprotein synthesisR01GM068077 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI COPELAND, PAUL R · 2003 to 2007
$1.5M
Investigation of the SBP2-ribosome interaction in Sec incorporationF31GM081920 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI CABAN, KELVIN · 2007 to 2009
$85k
NIAID NIH HHS T32 AI007403NIAID NIH HHS T32AI007403NIGMS NIH HHS F31 GM081920NIGMS NIH HHS F31GM081920NIGMS NIH HHS GM068077NIGMS NIH HHS GM077073NIGMS NIH HHS R01 GM068077NIGMS NIH HHS R01 GM077073
6 · The paper itself

Abstract

Selenocysteine (Sec) is incorporated at UGA codons in mRNAs possessing a Sec insertion sequence (SECIS) element in their 3'-untranslated region. At least three additional factors are necessary for Sec incorporation: SECIS-binding protein 2 (SBP2), Sec-tRNA(Sec), and a Sec-specific translation elongation factor (eEFSec). The C-terminal half of SBP2 is sufficient to promote Sec incorporation in vitro, which is carried out by the concerted action of a novel Sec incorporation domain and an L7Ae RNA-binding domain. Using alanine scanning mutagenesis, we show that two distinct regions of the Sec incorporation domain are required for Sec incorporation. Physical separation of the Sec incorporation and RNA-binding domains revealed that they are able to function in trans and established a novel role of the Sec incorporation domain in promoting SECIS and eEFSec binding to the SBP2 RNA-binding domain. We propose a model in which SECIS binding induces a conformational change in SBP2 that recruits eEFSec, which in concert with the Sec incorporation domain gains access to the ribosomal A site.

Indexed as

3' Untranslated RegionsAlanineAmino Acid SequenceHumansMolecular Sequence DataMutagenesisMutationPeptide Elongation FactorsProtein BindingProtein Structure, TertiaryRecombinant ProteinsRibosomesRNA-Binding ProteinsSelenocysteineSequence Homology, Amino Acid3' Untranslated RegionsAlanineEEFSEC protein, humanPeptide Elongation FactorsRecombinant ProteinsRNA-Binding ProteinsSECISBP2 protein, humanSelenocysteine

Identifiers

PMID18948268
PMCPMC3073842
OpenAlexW2058292954

What OpenQuestion holds

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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.