Evidence map›Paper›PMID 26007657›Full record

ArticleNucleic acids research2015

Two mechanisms coordinate replication termination by the Escherichia coli Tus-Ter complex.

Manjula Pandey, Mohamed M Elshenawy, Slobodan Jergic, Masateru Takahashi, Nicholas E Dixon, Samir M Hamdan, Smita S Patel

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

Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

13 citing papers in PubMed, 21 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Delineation of the Ancestral Tus-Dependent Replication Fork Trap.International journal of molecular sciences · 2021
    Article
  6. Review
  7. Article
  8. Dynamic structure mediates halophilic adaptation of a DNA polymerase from the deep-sea brines of the Red Sea.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2018
    Article
  9. Article
  10. Cryo-EM structure of the replisome reveals multiple interactions coordinating DNA synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  11. Review
  12. Article
  13. 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

7 authors at 3 institutions in 3 countries.

Manjula PandeyDepartment of Biochemistry and Molecular Biology, Rutgers, the State University of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA pandeyma@rwjms.rutgers.edu.
Mohamed M ElshenawyDivision of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, Thuwal 23955, Saudi Arabia.
Slobodan JergicCentre for Medical and Molecular Bioscience, University of Wollongong, New South Wales 2522, Australia.
Masateru TakahashiDivision of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, Thuwal 23955, Saudi Arabia.
Nicholas E DixonCentre for Medical and Molecular Bioscience, University of Wollongong, New South Wales 2522, Australia nickd@uow.edu.au.
Samir M HamdanDivision of Biological and Environmental Sciences and Engineering, King Abdullah University of Science and Technology, Thuwal 23955, Saudi Arabia.
Smita S PatelDepartment of Biochemistry and Molecular Biology, Rutgers, the State University of New Jersey, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA patelss@rutgers.edu.
King Abdullah University of Science and Technology · SARutgers, The State University of New Jersey · USUniversity of Wollongong · AU

Funding

MECHANISTIC STUDIES OF HEXAMERIC HELICASESR01GM055310 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PATEL, SMITA S · 1997 to 2015
$4.6M
NIGMS NIH HHS GM055310NIGMS NIH HHS R01 GM055310
6 · The paper itself

Abstract

The Escherichia coli replication terminator protein (Tus) binds to Ter sequences to block replication forks approaching from one direction. Here, we used single molecule and transient state kinetics to study responses of the heterologous phage T7 replisome to the Tus-Ter complex. The T7 replisome was arrested at the non-permissive end of Tus-Ter in a manner that is explained by a composite mousetrap and dynamic clamp model. An unpaired C(6) that forms a lock by binding into the cytosine binding pocket of Tus was most effective in arresting the replisome and mutation of C(6) removed the barrier. Isolated helicase was also blocked at the non-permissive end, but unexpectedly the isolated polymerase was not, unless C(6) was unpaired. Instead, the polymerase was blocked at the permissive end. This indicates that the Tus-Ter mechanism is sensitive to the translocation polarity of the DNA motor. The polymerase tracking along the template strand traps the C(6) to prevent lock formation; the helicase tracking along the other strand traps the complementary G(6) to aid lock formation. Our results are consistent with the model where strand separation by the helicase unpairs the GC(6) base pair and triggers lock formation immediately before the polymerase can sequester the C(6) base.

Indexed as

DNA ReplicationBase PairingDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesEscherichia coli ProteinsModels, Geneticbacteriophage T7 induced DNA polymeraseDNADNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA replication terminus site-binding protein, E coliEscherichia coli Proteinstus protein, E coli

Identifiers

PMID26007657
PMCPMC4499146
OpenAlexW2108034453

What OpenQuestion holds

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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.