Evidence map›Paper›PMID 26206669›Full record

ArticleNucleic acids research2015

The La-related protein 1-specific domain repurposes HEAT-like repeats to directly bind a 5'TOP sequence.

Roni M Lahr, Seshat M Mack, Annie Héroux, Sarah P Blagden, Cécile Bousquet-Antonelli, Jean-Marc Deragon, Andrea J Berman

Abstract read
In one paragraph

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
–field-weighted citation impact
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

46 citing papers in PubMed.

  1. Review
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  14. Phosphoprotein Profile of Rice (Plants (Basel, Switzerland) · 2022
    Article
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  18. Review
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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.

Roni M LahrDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Seshat M MackDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Annie HérouxPhoton Sciences Directorate, Bldg 745 L107 Brookhaven National Laboratory Upton, NY 11973, USA.
Sarah P BlagdenDepartment of Oncology, University of Oxford, Churchill Hospital, Oxford, OX3 7LE, UK.
Cécile Bousquet-AntonelliCNRS-UMR5096 LGDP, 66860 Perpignan, France Université de Perpignan-UMR5096 LGDP, 66860 Perpignan, France.
Jean-Marc DeragonCNRS-UMR5096 LGDP, 66860 Perpignan, France Université de Perpignan-UMR5096 LGDP, 66860 Perpignan, France.
Andrea J BermanDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA ajb190@pitt.edu.

Funding

Macromolecular Crystallography at the National Synchrotron Light SourceP41GM103473 · NIGMS · BROOKHAVEN SCIENCE ASSOC-BROOKHAVEN LAB · PI SWEET, ROBERT M · 2012 to 2013
$4.9M
NIGMS NIH HHS 8P41GM103473-16
6 · The paper itself

Abstract

La-related protein 1 (LARP1) regulates the stability of many mRNAs. These include 5'TOPs, mTOR-kinase responsive mRNAs with pyrimidine-rich 5' UTRs, which encode ribosomal proteins and translation factors. We determined that the highly conserved LARP1-specific C-terminal DM15 region of human LARP1 directly binds a 5'TOP sequence. The crystal structure of this DM15 region refined to 1.86 Å resolution has three structurally related and evolutionarily conserved helix-turn-helix modules within each monomer. These motifs resemble HEAT repeats, ubiquitous helical protein-binding structures, but their sequences are inconsistent with consensus sequences of known HEAT modules, suggesting this structure has been repurposed for RNA interactions. A putative mTORC1-recognition sequence sits within a flexible loop C-terminal to these repeats. We also present modelling of pyrimidine-rich single-stranded RNA onto the highly conserved surface of the DM15 region. These studies lay the foundation necessary for proceeding toward a structural mechanism by which LARP1 links mTOR signalling to ribosome biogenesis.

Indexed as

5' Untranslated RegionsAmino Acid MotifsAmino Acid SequenceAutoantigensConserved SequenceHelix-Turn-Helix MotifsHumansModels, MolecularRepetitive Sequences, Amino AcidRibonucleoproteinsRNA, MessengerSS-B AntigenStatic Electricity5' Untranslated RegionsAutoantigensRibonucleoproteinsRNA, MessengerSS-B Antigen

Identifiers

PMID26206669
PMCPMC4652764

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.