Evidence map›Paper›PMID 26324908›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Assembly, translocation, and activation of XerCD-dif recombination by FtsK translocase analyzed in real-time by FRET and two-color tethered fluorophore motion.

Peter F J May, Pawel Zawadzki, David J Sherratt, Achillefs N Kapanidis, Lidia K Arciszewska

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. The TLCΦ satellite phage harbors a Xer recombination activation factor.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  3. Review
  4. Article
  5. Tethered multifluorophore motion reveals equilibrium transition kinetics of single DNA double helices.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Review
  7. Review
  8. Article
  9. How Xer-exploiting mobile elements overcome cellular control.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  10. FtsK translocation permits discrimination between an endogenous and an imported Xer/dif recombination complex.Proceedings of the National Academy of Sciences of the United States of America · 2016
    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

5 authors at 1 institution in 1 country.

Peter F J MayBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom;
Pawel ZawadzkiDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
David J SherrattDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom.
Achillefs N KapanidisBiological Physics Research Group, Clarendon Laboratory, Department of Physics, University of Oxford, Oxford OX1 3PU, United Kingdom; a.kapanidis1@physics.ox.ac.uk lidia.arciszewska@bioch.ox.ac.uk.
Lidia K ArciszewskaDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, United Kingdom a.kapanidis1@physics.ox.ac.uk lidia.arciszewska@bioch.ox.ac.uk.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/H01795X/1European Research Council 261227Wellcome Trust 099204/Z/12Z
6 · The paper itself

Abstract

The FtsK dsDNA translocase functions in bacterial chromosome unlinking by activating XerCD-dif recombination in the replication terminus region. To analyze FtsK assembly and translocation, and the subsequent activation of XerCD-dif recombination, we extended the tethered fluorophore motion technique, using two spectrally distinct fluorophores to monitor two effective lengths along the same tethered DNA molecule. We observed that FtsK assembled stepwise on DNA into a single hexamer, and began translocation rapidly (∼ 0.25 s). Without extruding DNA loops, single FtsK hexamers approached XerCD-dif and resided there for ∼ 0.5 s irrespective of whether XerCD-dif was synapsed or unsynapsed. FtsK then dissociated, rather than reversing. Infrequently, FtsK activated XerCD-dif recombination when it encountered a preformed synaptic complex, and dissociated before the completion of recombination, consistent with each FtsK-XerCD-dif encounter activating only one round of recombination.

Indexed as

Adenosine TriphosphateBase SequenceChromosomes, BacterialDNAEscherichia coliEscherichia coli ProteinsFluorescence Resonance Energy TransferFluorescent DyesIntegrasesLikelihood FunctionsMembrane ProteinsMolecular Sequence DataMutagenesis, Site-DirectedNormal DistributionProtein BindingProtein TransportAdenosine TriphosphateDNAEscherichia coli ProteinsFluorescent DyesFtsK protein, E coliIntegrasesMembrane ProteinsXerC protein, E coliXerD protein, E colichromosome segregationDNA translocationsingle-molecule FRETsite-specific DNA recombinationtethered fluorophore motion

Identifiers

PMID26324908
PMCPMC4577173
OpenAlexW1927571466

What OpenQuestion holds

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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.