Evidence map›Paper›PMID 30215760›Full record

ArticleNucleic acids research2018

How to fold and protect mitochondrial ribosomal RNA with fewer guanines.

Maryam Hosseini, Poorna Roy, Marie Sissler, Craig L Zirbel, Eric Westhof, Neocles Leontis

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. The life and death of RNA across temperatures.Computational and structural biotechnology journal · 2022
    Review
  7. Mitoribosome assembly comes into view.Nature structural & molecular biology · 2021
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. 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

6 authors at 4 institutions in 2 countries.

Maryam HosseiniDepartment of Chemistry, Bowling Green State University, Bowling Green, OH 43403, USA.
Poorna RoyCenter for RNA Biomedicine, Department of Chemistry, University of Michigan, Ann Arbor, MI 48109-1055, USA.
Marie SisslerArchitecture et Réactivité de l'ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg France.
Craig L ZirbelDepartment of Mathematics and Statistics, Bowling Green State University, Bowling Green, OH 43403, USA.
Eric WesthofArchitecture et Réactivité de l'ARN, Université de Strasbourg, Institut de Biologie Moléculaire et Cellulaire du CNRS, Strasbourg France.
Neocles LeontisDepartment of Chemistry, Bowling Green State University, Bowling Green, OH 43403, USA.
Bowling Green State University · USCentre National de la Recherche Scientifique · FRInstitut de Biologie Moléculaire et Cellulaire · FRUniversity of Michigan–Ann Arbor · US

Funding

RNA 3D Motif Search, Atlas, and Prediction from SequenceR01GM085328 · NIGMS · BOWLING GREEN STATE UNIVERSITY · PI ZIRBEL, CRAIG L · 2010 to 2023
$4.0M
NIGMS NIH HHS R01 GM085328
6 · The paper itself

Abstract

Mammalian mitochondrial ribosomes evolved from bacterial ribosomes by reduction of ribosomal RNAs, increase of ribosomal protein content, and loss of guanine nucleotides. Guanine is the base most sensitive to oxidative damage. By systematically comparing high-quality, small ribosomal subunit RNA sequence alignments and solved 3D ribosome structures from mammalian mitochondria and bacteria, we deduce rules for folding a complex RNA with the remaining guanines shielded from solvent. Almost all conserved guanines in both bacterial and mammalian mitochondrial ribosomal RNA form guanine-specific, local or long-range, RNA-RNA or RNA-protein interactions. Many solvent-exposed guanines conserved in bacteria are replaced in mammalian mitochondria by bases less sensitive to oxidation. New guanines, conserved only in the mitochondrial alignment, are strategically positioned at solvent inaccessible sites to stabilize the ribosomal RNA structure. New mitochondrial proteins substitute for truncated RNA helices, maintain mutual spatial orientations of helices, compensate for lost RNA-RNA interactions, reduce solvent accessibility of bases, and replace guanines conserved in bacteria by forming specific amino acid-RNA interactions.

Indexed as

RNA FoldingAnimalsBase SequenceEscherichia coliGuanineMitochondriaModels, MolecularNucleic Acid ConformationProtein BindingRibosomal ProteinsRibosomesRNA, BacterialRNA, MitochondrialRNA, RibosomalSus scrofaGuanineRibosomal ProteinsRNA, BacterialRNA, MitochondrialRNA, Ribosomal

Identifiers

PMID30215760
PMCPMC6237812
OpenAlexW2890015074

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.