Evidence map›Paper›PMID 19013274›Full record

ArticleCell2008

Structural synergy and molecular crosstalk between bacterial helicase loaders and replication initiators.

Melissa L Mott, Jan P Erzberger, Mary M Coons, James M Berger

Abstract read
In one paragraph

Article in Cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.

0numbers the graph read from it
0cells of the map it votes in
79citing papers in PubMed
–field-weighted citation impact
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

79 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Open biology · 2020
    Review
  10. Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. A structural view of the initiators for chromosome replication.Current opinion in structural biology · 2018
    Review
  17. Article
  18. Review
  19. Article
  20. Review

19 more citing papers are in PubMed but not listed here.

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.

Melissa L MottMolecular and Cell Biology Department, Quantitative Biosciences Institute, University of California, Berkeley, CA 94720, USA.
Jan P Erzberger
Mary M Coons
James M Berger

Funding

Mechanistic Studies of Replication Initiation in ProkaryotesR37GM071747 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI James M. Berger · 2017 to 2026
$4.4M
Structure/Function Studies of DNA Replication InitiationR01GM071747 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 2005 to 2016
$4.0M
NIGMS NIH HHS R01 GM071747NIGMS NIH HHS R37 GM071747
6 · The paper itself

Abstract

The loading of oligomeric helicases onto replication origins marks an essential step in replisome assembly. In cells, dedicated AAA+ ATPases regulate loading, however, the mechanism by which these factors recruit and deposit helicases has remained unclear. To better understand this process, we determined the structure of the ATPase region of the bacterial helicase loader DnaC from Aquifex aeolicus to 2.7 A resolution. The structure shows that DnaC is a close paralog of the bacterial replication initiator, DnaA, and unexpectedly shares an ability to form a helical assembly similar to that of ATP-bound DnaA. Complementation and ssDNA-binding assays validate the importance of homomeric DnaC interactions, while pull-down experiments show that the DnaC and DnaA AAA+ domains interact in a nucleotide-dependent manner. These findings implicate DnaC as a molecular adaptor that uses ATP-activated DnaA as a docking site for regulating the recruitment and correct spatial deposition of the DnaB helicase onto origins.

Indexed as

DNA ReplicationAdenosine TriphosphatasesAmino Acid SequenceBacteriaBacterial ProteinsCrystallography, X-RayDnaB HelicasesDNA-Binding ProteinsDNA HelicasesDNA, Single-StrandedEscherichia coli ProteinsModels, BiologicalMolecular Sequence DataProtein BindingProtein ConformationSequence Homology, Amino AcidAdenosine TriphosphatasesBacterial ProteinsDnaA protein, BacteriaDnaB HelicasesDNA-Binding ProteinsDnaC protein, E coliDNA HelicasesDNA, Single-StrandedEscherichia coli Proteins

Identifiers

PMID19013274
PMCPMC2610854

What OpenQuestion holds

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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.