Evidence map›Paper›PMID 25745110›Full record

ArticleThe Journal of biological chemistry2015

Identification of Subunit Binding Positions on a Model Fork and Displacements That Occur during Sequential Assembly of the Escherichia coli Primosome.

Carol M Manhart, Charles S McHenry

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

11 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Structure-specific DNA replication-fork recognition directs helicase and replication restart activities of the PriA helicase.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  6. Review
  7. Article
  8. 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

2 authors at 1 institution in 1 country.

Carol M ManhartFrom the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80303.
Charles S McHenryFrom the Department of Chemistry and Biochemistry, University of Colorado, Boulder, Colorado 80303 charles.mchenry@colorado.edu.
University of Colorado Boulder · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

When replication stalls and forks disassemble, the restart primosome is required to reload the replicative helicase so that chromosomal replication can be reinitiated. We have taken a photo-cross-linking approach, using model replication forks containing a phenyl diazirine placed at single locations, to determine the positions of primosomal protein binding and changes in interactions that occur during the assembly reaction. This approach revealed a novel mode for single-stranded DNA-binding protein (SSB)-DNA binding, in which SSB interacts with both the leading and lagging single-strand segments and the parental duplex of the fork. Cross-linking to a novel region within SSB is observed only when it is bound to forked structures. This binding mode is also followed by PriB. PriA binds to the fork, excluding SSB and PriB, interacting with the primer terminus, single-stranded leading and lagging strands and duplex in immediate proximity of the fork. SSB binds to flanking single-stranded segments distal to the fork in the presence of PriA. The addition of PriB or DnaT to a PriA-SSB-fork complex does not lead to cross-linking or displacement, suggesting that their association is through protein-protein interactions at early stages of the reaction. Upon addition of DnaC and the DnaB helicase in the presence of ATPγS, helicase is assembled, leading to contacts within the duplex region on the tracking (lagging) strand and strong contacts with the displaced leading single strand near the fork. PriA is displaced from DNA upon helicase assembly.

Indexed as

Base SequenceBinding SitesDNA, BacterialDnaB HelicasesDNA-Binding ProteinsDNA HelicasesDNA ReplicationDNA, Single-StrandedEscherichia coliEscherichia coli ProteinsModels, BiologicalMolecular Sequence DataProtein SubunitsDNA, BacterialDnaB HelicasesDNA-Binding ProteinsdnaB protein, E coliDNA HelicasesDNA, Single-StrandedDnaT protein, E coliEscherichia coli ProteinspriA protein, E coliPriB protein, E coliProtein SubunitsSSB protein, E coliDiazirineDNA Binding ProteinDNA HelicaseDNA-Protein InteractionDNA ReplicationEnzyme MechanismHelicasePhoto-cross-linkingPriAPrimosome5

Identifiers

PMID25745110
PMCPMC4409247
OpenAlexW2094572057

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.