Evidence map›Paper›PMID 27056333›Full record

ArticleThe Journal of biological chemistry2016

DNA Polymerase III, but Not Polymerase IV, Must Be Bound to a τ-Containing DnaX Complex to Enable Exchange into Replication Forks.

Quan Yuan, Paul R Dohrmann, Mark D Sutton, Charles S McHenry

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. 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
1.9field-weighted citation impact, top 14% 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, 22 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Direct visualization of translesion DNA synthesis polymerase IV at the replisome.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Article
  6. Article
  7. Article
  8. A gatekeeping function of the replicative polymerase controls pathway choice in the resolution of lesion-stalled replisomes.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  9. Article
  10. Review
  11. Article
  12. Article
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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

4 authors at 2 institutions in 1 country.

Quan YuanFrom the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80303 and.
Paul R DohrmannFrom the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80303 and.
Mark D Suttonthe Department of Biochemistry, Jacobs School of Medicine and Biomedical Sciences, State University of New York, Buffalo, New York 14214.
Charles S McHenryFrom the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80303 and charles.mchenry@colorado.edu.
University of Colorado Boulder · USUniversity at Buffalo, State University of New York · US

Funding

Regulation of DNA Replication and RepairR01GM066094 · NIGMS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SUTTON, MARK D. · 2003 to 2016
$4.0M
NIGMS NIH HHS R01 GM066094
6 · The paper itself

Abstract

Examples of dynamic polymerase exchange have been previously characterized in model systems provided by coliphages T4 and T7. Using a dominant negative D403E polymerase (Pol) III α that can form initiation complexes and sequester primer termini but not elongate, we investigated the possibility of exchange at the Escherichia coli replication fork on a rolling circle template. Unlike other systems, addition of polymerase alone did not lead to exchange. Only when D403E Pol III was bound to a τ-containing DnaX complex did exchange occur. In contrast, addition of Pol IV led to rapid exchange in the absence of bound DnaX complex. Examination of Pol III* with varying composition of τ or the alternative shorter dnaX translation product γ showed that τ-, τ2-, or τ3-DnaX complexes supported equivalent levels of synthesis, identical Okazaki fragment size, and gaps between fragments, possessed the ability to challenge pre-established replication forks, and displayed equivalent susceptibility to challenge by exogenous D403E Pol III*. These findings reveal that redundant interactions at the replication fork must stabilize complexes containing only one τ. Previously, it was thought that at least two τs in the trimeric DnaX complex were required to couple the leading and lagging strand polymerases at the replication fork. Possible mechanisms of exchange are discussed.

Indexed as

DNA ReplicationBacterial ProteinsDNA, BacterialDNA Polymerase betaDNA Polymerase IIIElectrophoresis, Agar GelEscherichia coliBacterial ProteinsDNA, BacterialDNA Polymerase betaDNA Polymerase IIIDnaX protein, Bacteriaclamp loaderDNA helicaseDNA polymeraseDnaX complexdynamic processivitygenomic instabilitynucleic acid enzymologypolymerase exchangeprotein-DNA interactionreplication fork

Identifiers

PMID27056333
PMCPMC4882441
OpenAlexW2319364552

What OpenQuestion holds

Textmetadata
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.