Evidence map›Paper›PMID 29146908›Full record

ArticleNature communications2017

LRPPRC-mediated folding of the mitochondrial transcriptome.

Stefan J Siira, Henrik Spåhr, Anne-Marie J Shearwood, Benedetta Ruzzenente, Nils-Göran Larsson, Oliver Rackham, Aleksandra Filipovska

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 5% 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

76 citing papers in PubMed, 1 synthesis or guideline pooled it, 118 citations in OpenAlex.

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16 more citing papers are in PubMed but not listed here.

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.

Stefan J SiiraHarry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia.
Henrik SpåhrDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, D-50931, Cologne, Germany.
Anne-Marie J ShearwoodHarry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia.
Benedetta RuzzenenteDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, D-50931, Cologne, Germany.
Nils-Göran LarssonDepartment of Mitochondrial Biology, Max Planck Institute for Biology of Ageing, D-50931, Cologne, Germany.
Oliver RackhamHarry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia. oliver.rackham@uwa.edu.au.ORCID http://orcid.org/0000-0002-5301-9624
Aleksandra FilipovskaHarry Perkins Institute of Medical Research and Centre for Medical Research, The University of Western Australia, Nedlands, WA, 6009, Australia. aleksandra.filipovska@uwa.edu.au.
The University of Western Australia · AUDélégation Paris 5 · FRKarolinska Institutet · SEMax Planck Institute for Biology of Ageing · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The expression of the compact mammalian mitochondrial genome requires transcription, RNA processing, translation and RNA decay, much like the more complex chromosomal systems, and here we use it as a model system to understand the fundamental aspects of gene expression. Here we combine RNase footprinting with PAR-CLIP at unprecedented depth to reveal the importance of RNA-protein interactions in dictating RNA folding within the mitochondrial transcriptome. We show that LRPPRC, in complex with its protein partner SLIRP, binds throughout the mitochondrial transcriptome, with a preference for mRNAs, and its loss affects the entire secondary structure and stability of the transcriptome. We demonstrate that the LRPPRC-SLIRP complex is a global RNA chaperone that stabilizes RNA structures to expose the required sites for translation, stabilization, and polyadenylation. Our findings reveal a general mechanism where extensive RNA-protein interactions ensure that RNA is accessible for its biological functions.

Indexed as

AnimalsBinding SitesFibroblastsGenome, MitochondrialHumansMaleMice, Inbred C57BLMice, KnockoutMitochondriaMolecular ChaperonesNeoplasm ProteinsPolyadenylationProtein BindingProtein BiosynthesisProtein FootprintingRecombinant ProteinsLRPPRC protein, humanLrpprc protein, mouseMolecular ChaperonesNeoplasm ProteinsRecombinant ProteinsRNA-Binding ProteinsRNA, MessengerSLIRP protein, humanSLIRP protein, mouse

Identifiers

PMID29146908
PMCPMC5691074
OpenAlexW2767740853

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.