Evidence map›Paper›PMID 25609698›Full record

ArticleNucleic acids research2015

The solution structure of the pentatricopeptide repeat protein PPR10 upon binding atpH RNA.

Benjamin S Gully, Nathan Cowieson, Will A Stanley, Kate Shearston, Ian D Small, Alice Barkan, Charles S Bond

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 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing 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

37 citing papers in PubMed.

  1. Article
  2. Review
  3. Structures of pentatricopeptide repeat proteins.Acta crystallographica. Section F, Structural biology communications · 2026
    Review
  4. Review
  5. Article
  6. Review
  7. PPR596 Is Required forInternational journal of molecular sciences · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Fine mapping ofBreeding science · 2022
    Article
  12. International journal of molecular sciences · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. The Mitochondrial Pentatricopeptide Repeat Protein PPR18 Is Required for theInternational journal of molecular sciences · 2020
    Article
  18. Article
  19. Article
  20. Programmable RNA manipulation in living cells.Cellular and molecular life sciences : CMLS · 2019
    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.

Benjamin S GullySchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia.
Nathan CowiesonSAXSWAXS beamline, Australian Synchrotron, 800 Blackburn Road, Clayton, Victoria, Australia.
Will A StanleySchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
Kate ShearstonSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Australian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
Ian D SmallAustralian Research Council Centre of Excellence in Plant Energy Biology, The University of Western Australia, Crawley, Western Australia, Australia.
Alice BarkanInstitute of Molecular Biology, University of Oregon, Eugene, Oregon, USA.
Charles S BondSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, Western Australia, Australia Charles.Bond@uwa.edu.au.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The pentatricopeptide repeat (PPR) protein family is a large family of RNA-binding proteins that is characterized by tandem arrays of a degenerate 35-amino-acid motif which form an α-solenoid structure. PPR proteins influence the editing, splicing, translation and stability of specific RNAs in mitochondria and chloroplasts ZEA MAYS: PPR10 is amongst the best studied PPR proteins, where sequence-specific binding to two RNA transcripts, ATPH: and PSAJ, HAS BEEN DEMONSTRATED TO FOLLOW: a recognition code where the identity of two amino acids per repeat determines the base-specificity. A recently solved ZmPPR10: PSAJ: complex crystal structure suggested a homodimeric complex with considerably fewer sequence-specific protein-RNA contacts than inferred PREVIOUSLY: Here we describe the solution structure of the ZmPPR10: ATPH: complex using size-exclusion chromatography-coupled synchrotron small-angle X-ray scattering (SEC-SY-SAXS). Our results support prior evidence that PPR10 binds RNA as a monomer, and that it does so in a manner that is commensurate with a canonical and predictable RNA-binding mode across much of the RNA-protein interface.

Indexed as

Circular DichroismModels, MolecularPlant ProteinsRNA, PlantScattering, RadiationZea maysPlant ProteinsRNA, Plant

Identifiers

PMID25609698
PMCPMC4330388

What OpenQuestion holds

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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.