Evidence map›Paper›PMID 20723756›Full record

ArticleCell2010

PcrA helicase dismantles RecA filaments by reeling in DNA in uniform steps.

Jeehae Park, Sua Myong, Anita Niedziela-Majka, Kyung Suk Lee, Jin Yu, Timothy M Lohman, Taekjip Ha

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 124 papers.

0numbers the graph read from it
0cells of the map it votes in
124citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

124 citing papers in PubMed, 170 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. The Role of SF1 and SF2 Helicases in Biotechnological Applications.Applied biochemistry and biotechnology · 2024
    Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Sequence-dependent mechanochemical coupling of helicase translocation and unwinding at single-nucleotide resolution.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  12. Review
  13. Article
  14. Article
  15. Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

64 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

7 authors at 4 institutions in 1 country.

Jeehae ParkCenter for Biophysics and Computational Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.
Sua Myong
Anita Niedziela-Majka
Kyung Suk Lee
Jin Yu
Timothy M Lohman
Taekjip Ha
University of Illinois Urbana-Champaign · USWashington University in St. Louis · USHoward Hughes Medical Institute · USUniversity of California, Berkeley · US

Funding

HELICASE-CATALYZED DNA UNWINDINGR01GM045948 · NIGMS · WASHINGTON UNIVERSITY · PI LOHMAN, TIMOTHY M · 1991 to 2020
$9.2M
Single Molecule Study of Helicase MechanismsR01GM065367 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HA, TAEKJIP · 2002 to 2014
$3.6M
Howard Hughes Medical InstituteNIGMS NIH HHS GM-045948NIGMS NIH HHS GM-065367NIGMS NIH HHS R01 GM045948NIGMS NIH HHS R01 GM065367
6 · The paper itself

Abstract

Translocation of helicase-like proteins on nucleic acids underlies key cellular functions. However, it is still unclear how translocation can drive removal of DNA-bound proteins, and basic properties like the elementary step size remain controversial. Using single-molecule fluorescence analysis on a prototypical superfamily 1 helicase, Bacillus stearothermophilus PcrA, we discovered that PcrA preferentially translocates on the DNA lagging strand instead of unwinding the template duplex. PcrA anchors itself to the template duplex using the 2B subdomain and reels in the lagging strand, extruding a single-stranded loop. Static disorder limited previous ensemble studies of a PcrA stepping mechanism. Here, highly repetitive looping revealed that PcrA translocates in uniform steps of 1 nt. This reeling-in activity requires the open conformation of PcrA and can rapidly dismantle a preformed RecA filament even at low PcrA concentrations, suggesting a mode of action for eliminating potentially deleterious recombination intermediates.

Indexed as

DNA ReplicationBacterial ProteinsDNA HelicasesDNA, Single-StrandedFluorescenceGeobacillus stearothermophilusKineticsModels, MolecularRec A RecombinasesBacterial ProteinsDNA HelicasesDNA, Single-StrandedpcrA protein, BacteriaRec A Recombinases

Identifiers

PMID20723756
PMCPMC2943210
OpenAlexW2059315855

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.