Evidence map›Paper›PMID 19414020›Full record

ArticleJournal of molecular biology2009

Structural and functional characterisation of a conserved archaeal RadA paralog with antirecombinase activity.

Anne-Marie McRobbie, Lester G Carter, Melina Kerou, Huanting Liu, Stephen A McMahon, Kenneth A Johnson, Muse Oke, James H Naismith, Malcolm F White

Abstract read
In one paragraph

Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

17 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Mediators of homologous DNA pairing.Cold Spring Harbor perspectives in biology · 2014
    Review
  11. Review
  12. Article
  13. Article
  14. Experimental phasing using zinc anomalous scattering.Acta crystallographica. Section D, Biological crystallography · 2012
    Article
  15. Article
  16. Article
  17. The Scottish Structural Proteomics Facility: targets, methods and outputs.Journal of structural and functional genomics · 2010
    Article
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

9 authors at 1 institution in 1 country.

Anne-Marie McRobbieCentre for Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews, Fife KY16 9ST, UK.
Lester G Carter
Melina Kerou
Huanting Liu
Stephen A McMahon
Kenneth A Johnson
Muse Oke
James H Naismith
Malcolm F White
University of St Andrews · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/B/14426Medical Research Council G0500367
6 · The paper itself

Abstract

DNA recombinases (RecA in bacteria, Rad51 in eukarya and RadA in archaea) catalyse strand exchange between homologous DNA molecules, the central reaction of homologous recombination, and are among the most conserved DNA repair proteins known. RecA is the sole protein responsible for this reaction in bacteria, whereas there are several Rad51 paralogs that cooperate to catalyse strand exchange in eukaryotes. All archaea have at least one (and as many as four) RadA paralog, but their function remains unclear. Herein, we show that the three RadA paralogs encoded by the Sulfolobus solfataricus genome are expressed under normal growth conditions and are not UV inducible. We demonstrate that one of these proteins, Sso2452, which is representative of the large archaeal RadC subfamily of archaeal RadA paralogs, functions as an ATPase that binds tightly to single-stranded DNA. However, Sso2452 is not an active recombinase in vitro and inhibits D-loop formation by RadA. We present the high-resolution crystal structure of Sso2452, which reveals key structural differences from the canonical RecA family recombinases that may explain its functional properties. The possible roles of the archaeal RadA paralogs in vivo are discussed.

Indexed as

Archaeal ProteinsCrystallography, X-RayDNA-Binding ProteinsHumansIsoenzymesModels, MolecularMolecular Sequence DataNucleic Acid ConformationPhylogenyProtein Structure, QuaternaryRecombinasesSequence AlignmentSulfolobus solfataricusArchaeal ProteinsDNA-Binding ProteinsIsoenzymesRadA protein, archaealRecombinases

Identifiers

PMID19414020
PMCPMC3387904
OpenAlexW1981102842

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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.