Evidence map›Paper›PMID 24214995›Full record

ArticleNucleic acids research2014

TPM analyses reveal that FtsK contributes both to the assembly and the activation of the XerCD-dif recombination synapse.

Cheikh Tidiane Diagne, Maya Salhi, Estelle Crozat, Laurence Salomé, Francois Cornet, Philippe Rousseau, Catherine Tardin

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2014. 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
1.8field-weighted citation impact, top 15% 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, 31 citations in OpenAlex.

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  13. 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
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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 at 4 institutions in 1 country.

Cheikh Tidiane DiagneCNRS; IPBS (Institut de Pharmacologie et de Biologie Structurale); 205 route de Narbonne BP 64182, F-31077 Toulouse, France, Université de Toulouse; UPS; IPBS; F-31077 Toulouse, France, Université de Toulouse; UPS; LMGM (Laboratoire de Microbiologie et Génétique Moléculaires); F-31062 Toulouse, France and CNRS; LMGM; F-31062 Toulouse, France.
Maya Salhi
Estelle Crozat
Laurence Salomé
Francois Cornet
Philippe Rousseau
Catherine Tardin
Centre National de la Recherche Scientifique · FRLaboratoire de Microbiologie et Génétique Moléculaires · FRUniversité Toulouse III - Paul Sabatier · FRInstitut de Pharmacologie et de Biologie Structurale · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Circular chromosomes can form dimers during replication and failure to resolve those into monomers prevents chromosome segregation, which leads to cell death. Dimer resolution is catalysed by a highly conserved site-specific recombination system, called XerCD-dif in Escherichia coli. Recombination is activated by the DNA translocase FtsK, which is associated with the division septum, and is thought to contribute to the assembly of the XerCD-dif synapse. In our study, direct observation of the assembly of the XerCD-dif synapse, which had previously eluded other methods, was made possible by the use of Tethered Particle Motion, a single molecule approach. We show that XerC, XerD and two dif sites suffice for the assembly of XerCD-dif synapses in absence of FtsK, but lead to inactive XerCD-dif synapses. We also show that the presence of the γ domain of FtsK increases the rate of synapse formation and convert them into active synapses where recombination occurs. Our results represent the first direct observation of the formation of the XerCD-dif recombination synapse and its activation by FtsK.

Indexed as

Recombination, GeneticEscherichia coli ProteinsIntegrasesKineticsMembrane ProteinsMotionProtein Structure, TertiaryEscherichia coli ProteinsFtsK protein, E coliIntegrasesMembrane ProteinsXerC protein, E coliXerD protein, E coli

Identifiers

PMID24214995
PMCPMC3919580
OpenAlexW2107350483

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.