Evidence map›Paper›PMID 18631376›Full record

ArticleBMC plant biology2008

Correlation between amino acid residues converted by RNA editing and functional residues in protein three-dimensional structures in plant organelles.

Kei Yura, Mitiko Go

Open access · goldAbstract read
In one paragraph

Article in BMC plant biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.9field-weighted citation impact, top 15% of its field
1 · What the graph read from it

What it found

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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

36 citing papers in PubMed, 57 citations in OpenAlex.

  1. Structural divergence and molecular adaptation ofFrontiers in plant science · 2026
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  2. Comprehensive plastome variation and RNA editing inFrontiers in plant science · 2026
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  8. The organelle genomes of the endangered seagrassFrontiers in plant science · 2025
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  16. Article
  17. A study of RNA-editing inForestry research · 2021
    Article
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  19. Article
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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

2 authors at 2 institutions in 1 country.

Kei YuraGraduate School of Humanities and Sciences, Ochanomizu University, 2-1-1, Otsuka, Bunkyo, Tokyo 112-8610, Japan. yura.kei@ocha.ac.jp
Mitiko Go
Ochanomizu University · JPOtsuka (Japan) · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundIn plant organelles, specific messenger RNAs (mRNAs) are subjected to conversion editing, a process that often converts the first or second nucleotide of a codon and hence the encoded amino acid. No systematic patterns in converted sites were found on mRNAs, and the converted sites rarely encoded residues located at the active sites of proteins. The role and origin of RNA editing in plant organelles remain to be elucidated.

resultsHere we study the relationship between amino acid residues encoded by edited codons and the structural characteristics of these residues within proteins, e.g., in protein-protein interfaces, elements of secondary structure, or protein structural cores. We find that the residues encoded by edited codons are significantly biased toward involvement in helices and protein structural cores. RNA editing can convert codons for hydrophilic to hydrophobic amino acids. Hence, only the edited form of an mRNA can be translated into a polypeptide with helix-preferring and core-forming residues at the appropriate positions, which is often required for a protein to form a functional three-dimensional (3D) structure.

conclusionWe have performed a novel analysis of the location of residues affected by RNA editing in proteins in plant organelles. This study documents that RNA editing sites are often found in positions important for 3D structure formation. Without RNA editing, protein folding will not occur properly, thus affecting gene expression. We suggest that RNA editing may have conferring evolutionary advantage by acting as a mechanism to reduce susceptibility to DNA damage by allowing the increase in GC content in DNA while maintaining RNA codons essential to encode residues required for protein folding and activity.

Indexed as

RNA EditingAmino Acid SequenceCodonDatabases, Nucleic AcidMolecular Sequence DataOrganellesPlant ProteinsProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryRNA, MessengerRNA, PlantSequence Homology, Amino AcidCodonPlant ProteinsRNA, MessengerRNA, Plant

Identifiers

PMID18631376
PMCPMC2488346
OpenAlexW2017095627

What OpenQuestion holds

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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.