Evidence map›Paper›PMID 21911368›Full record

ArticleNucleic acids research2012

A conserved lysine residue of plant Whirly proteins is necessary for higher order protein assembly and protection against DNA damage.

Laurent Cappadocia, Jean-Sébastien Parent, Eric Zampini, Etienne Lepage, Jurgen Sygusch, Normand Brisson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Redox Signaling in Plant Heat Stress Response.Antioxidants (Basel, Switzerland) · 2023
    Review
  6. WHIRLY protein functions in plants.Food and energy security · 2023
    Review
  7. Article
  8. Review
  9. Plastid Genomes of Flowering Plants: Essential Principles.Methods in molecular biology (Clifton, N.J.) · 2021
    Article
  10. Article
  11. Article
  12. HCells · 2019
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

Laurent CappadociaDepartment of Biochemistry, Université de Montréal, CP 6128, Station Centre-Ville, Montréal H3C 3J7, Québec, Canada.
Jean-Sébastien Parent
Eric Zampini
Etienne Lepage
Jurgen Sygusch
Normand Brisson
Université de Montréal · CA

Funding

Case Center for Synchrotron BiosciencesP30EB009998 · NIBIB · CASE WESTERN RESERVE UNIVERSITY · PI CHANCE, MARK R · 2009 to 2018
$8.4M
CIHRNIBIB NIH HHS P30 EB009998
6 · The paper itself

Abstract

All organisms have evolved specialized DNA repair mechanisms in order to protect their genome against detrimental lesions such as DNA double-strand breaks. In plant organelles, these damages are repaired either through recombination or through a microhomology-mediated break-induced replication pathway. Whirly proteins are modulators of this second pathway in both chloroplasts and mitochondria. In this precise pathway, tetrameric Whirly proteins are believed to bind single-stranded DNA and prevent spurious annealing of resected DNA molecules with other regions in the genome. In this study, we add a new layer of complexity to this model by showing through atomic force microscopy that tetramers of the potato Whirly protein WHY2 further assemble into hexamers of tetramers, or 24-mers, upon binding long DNA molecules. This process depends on tetramer-tetramer interactions mediated by K67, a highly conserved residue among plant Whirly proteins. Mutation of this residue abolishes the formation of 24-mers without affecting the protein structure or the binding to short DNA molecules. Importantly, we show that an Arabidopsis Whirly protein mutated for this lysine is unable to rescue the sensitivity of a Whirly-less mutant plant to a DNA double-strand break inducing agent.

Indexed as

DNA DamageArabidopsisArabidopsis ProteinsCiprofloxacinDNA-Binding ProteinsDNA, Single-StrandedLysineMicroscopy, Atomic ForceModels, MolecularMutationPlant ProteinsProtein MultimerizationSolanum tuberosumArabidopsis ProteinsCiprofloxacinDNA-Binding ProteinsDNA, Single-StrandedLysinePlant ProteinsWhirly1 protein, ArabidopsisWhirly3 protein, Arabidopsis

Identifiers

PMID21911368
PMCPMC3245945
OpenAlexW2137418630

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.