Evidence map›Paper›PMID 27708355›Full record

ArticleScientific reports2016

Activation of Xer-recombination at dif: structural basis of the FtsKγ-XerD interaction.

Andrew N Keller, Yue Xin, Stephanie Boer, Jonathan Reinhardt, Rachel Baker, Lidia K Arciszewska, Peter J Lewis, David J Sherratt, Jan Löwe, Ian Grainge

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Dynamics in Cre-loxP site-specific recombination.Current opinion in structural biology · 2024
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. FtsK in motion reveals its mechanism for double-stranded DNA translocation.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Review
  12. 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
  13. Article
  14. Review
  15. 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

10 authors at 3 institutions in 2 countries.

Andrew N KellerSchool of Environmental and Life Sciences, University of Newcastle, University Drive, Callaghan NSW 2308, Australia.
Yue XinSchool of Environmental and Life Sciences, University of Newcastle, University Drive, Callaghan NSW 2308, Australia.
Stephanie BoerSchool of Environmental and Life Sciences, University of Newcastle, University Drive, Callaghan NSW 2308, Australia.
Jonathan ReinhardtDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Rachel BakerDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Lidia K ArciszewskaDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Peter J LewisSchool of Environmental and Life Sciences, University of Newcastle, University Drive, Callaghan NSW 2308, Australia.
David J SherrattDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Jan LöweMRC Laboratory of Molecular Biology, Francis Crick Avenue, Cambridge, CB2 2QH, United Kingdom.
Ian GraingeSchool of Environmental and Life Sciences, University of Newcastle, University Drive, Callaghan NSW 2308, Australia.
University of Newcastle Australia · AUUniversity of Oxford · GBMRC Laboratory of Molecular Biology · GB

Funding

Medical Research Council MC_U105184326Wellcome Trust 095514/Z/11/ZWellcome Trust 099204/Z/12ZWellcome Trust 200782/Z/16/Z
6 · The paper itself

Abstract

Bacterial chromosomes are most often circular DNA molecules. This can produce a topological problem; a genetic crossover from homologous recombination results in dimerization of the chromosome. A chromosome dimer is lethal unless resolved. A site-specific recombination system catalyses this dimer-resolution reaction at the chromosomal site dif. In Escherichia coli, two tyrosine-family recombinases, XerC and XerD, bind to dif and carry out two pairs of sequential strand exchange reactions. However, what makes the reaction unique among site-specific recombination reactions is that the first step, XerD-mediated strand exchange, relies on interaction with the very C-terminus of the FtsK DNA translocase. FtsK is a powerful molecular motor that functions in cell division, co-ordinating division with clearing chromosomal DNA from the site of septation and also acts to position the dif sites for recombination. This is a model system for unlinking, separating and segregating large DNA molecules. Here we describe the molecular detail of the interaction between XerD and FtsK that leads to activation of recombination as deduced from a co-crystal structure, biochemical and in vivo experiments. FtsKγ interacts with the C-terminal domain of XerD, above a cleft where XerC is thought to bind. We present a model for activation of recombination based on structural data.

Indexed as

Recombination, GeneticBase SequenceChromosomes, BacterialEscherichia coliEscherichia coli ProteinsIntegrasesMembrane ProteinsEscherichia coli ProteinsFtsK protein, E coliIntegrasesMembrane ProteinsXerC protein, E coliXerD protein, E coli

Identifiers

PMID27708355
PMCPMC5052618
OpenAlexW2529819952

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LicenceCC BY
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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.