Evidence map›Paper›PMID 23603827›Full record

ArticleRNA biology2013

Distinct binding properties of TIAR RRMs and linker region.

Henry S Kim, Stephen J Headey, Yano M K Yoga, Martin J Scanlon, Myriam Gorospe, Matthew C J Wilce, Jacqueline A Wilce

Open access · bronzeAbstract read
In one paragraph

Article in RNA biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. T-Cell Intracellular Antigen 1-Like Protein in Physiology and Pathology.International journal of molecular sciences · 2022
    Review
  7. eLife · 2021
    Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. T-cell intracellular antigens in health and disease.Cell cycle (Georgetown, Tex.) · 2015
    Review
  19. RNA recognition and stress granule formation by TIA proteins.International journal of molecular sciences · 2014
    Review
  20. 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

7 authors at 4 institutions in 4 countries.

Henry S KimDepartment of Biochemistry and Molecular Biology, Monash University, Victoria, Australia.
Stephen J Headey
Yano M K Yoga
Martin J Scanlon
Myriam Gorospe
Matthew C J Wilce
Jacqueline A Wilce
Australian Regenerative Medicine Institute · AUInstitute of Medicinal Plant Development · CNMonash University · AUNational Institute on Aging · US

Funding

Post-transcriptional Regulation Of Proliferative and Stress Response GenesZIAAG000511 · NIA · NATIONAL INSTITUTE ON AGING · PI GOROSPE, MYRIAM · 2009 to 2025
$25.4M
Intramural NIH HHS
6 · The paper itself

Abstract

The RNA-binding protein TIAR is an mRNA-binding protein that acts as a translational repressor, particularly important under conditions of cellular stress. It binds to target mRNA and DNA via its RNA recognition motif (RRM) domains and is involved in both splicing regulation and translational repression via the formation of "stress granules." TIAR has also been shown to bind ssDNA and play a role in the regulation of transcription. Here we show, using surface plasmon resonance and nuclear magnetic resonance spectroscopy, specific roles of individual TIAR domains for high-affinity binding to RNA and DNA targets. We confirm that RRM2 of TIAR is the major RNA- and DNA-binding domain. However, the strong nanomolar affinity binding to U-rich RNA and T-rich DNA depends on the presence of the six amino acid residues found in the linker region C-terminal to RRM2. On its own, RRM1 shows preferred binding to DNA over RNA. We further characterize the interaction between RRM2 with the C-terminal extension and an AU-rich target RNA sequence using NMR spectroscopy to identify the amino acid residues involved in binding. We demonstrate that TIAR RRM2, together with its C-terminal extension, is the major contributor for the high-affinity (nM) interactions of TIAR with target RNA sequences.

Indexed as

Amino Acid MotifsAmino Acid SequenceBinding SitesDNADNA-Binding ProteinsGene Expression RegulationHumansMagnetic Resonance SpectroscopyModels, MolecularProtein BindingRNA-Binding ProteinsRNA, MessengerRNA SplicingSequence AlignmentSurface Plasmon ResonanceDNADNA-Binding ProteinsRNA-Binding ProteinsRNA, MessengerTIAL1 protein, humanC-terminal extensionNMRRNA-binding proteinRRMsurface plasmon resonance (SPR)TIA-1TIARtranslational regulation

Identifiers

PMID23603827
PMCPMC3710364
OpenAlexW2030255427

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.