Evidence map›Paper›PMID 30649515›Full record

ArticleNucleic acids research2019

Determining the effects of DNA sequence on Hel308 helicase translocation along single-stranded DNA using nanopore tweezers.

Jonathan M Craig, Andrew H Laszlo, Ian C Nova, Henry Brinkerhoff, Matthew T Noakes, Katherine S Baker, Jasmine L Bowman, Hugh R Higinbotham, Jonathan W Mount, Jens H Gundlach

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Helicase HELQ: Molecular Characters Fit for DSB Repair Function.International journal of molecular sciences · 2024
    Review
  9. Article
  10. Nanopore tweezers show fractional-nucleotide translocation in sequence-dependent pausing by RNA polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Inhibition of the SARS-CoV-2 helicase at single-nucleotide resolution.bioRxiv : the preprint server for biology · 2022
    Article
  18. 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
  19. Review
  20. 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

10 authors at 1 institution in 1 country.

Jonathan M CraigDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Andrew H LaszloDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Ian C NovaDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Henry BrinkerhoffDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Matthew T NoakesDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Katherine S BakerDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Jasmine L BowmanDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Hugh R HiginbothamDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Jonathan W MountDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
Jens H GundlachDepartment of Physics, University of Washington, Seattle, WA 98105, USA.
University of Washington · US

Funding

Nanopore sequencing of DNA with MspAR01HG005115 · NHGRI · UNIVERSITY OF WASHINGTON · PI GUNDLACH, JENS, LASZLO, ANDREW · 2009 to 2024
$14.0M
NHGRI NIH HHS R01 HG005115
6 · The paper itself

Abstract

Motor enzymes that process nucleic-acid substrates play vital roles in all aspects of genome replication, expression, and repair. The DNA and RNA nucleobases are known to affect the kinetics of these systems in biologically meaningful ways. Recently, it was shown that DNA bases control the translocation speed of helicases on single-stranded DNA, however the cause of these effects remains unclear. We use single-molecule picometer-resolution nanopore tweezers (SPRNT) to measure the kinetics of translocation along single-stranded DNA by the helicase Hel308 from Thermococcus gammatolerans. SPRNT can measure enzyme steps with subangstrom resolution on millisecond timescales while simultaneously measuring the absolute position of the enzyme along the DNA substrate. Previous experiments with SPRNT revealed the presence of two distinct substates within the Hel308 ATP hydrolysis cycle, one [ATP]-dependent and the other [ATP]-independent. Here, we analyze in-depth the apparent sequence dependent behavior of the [ATP]-independent step. We find that DNA bases at two sites within Hel308 control sequence-specific kinetics of the [ATP]-independent step. We suggest mechanisms for the observed sequence-specific translocation kinetics. Similar SPRNT measurements and methods can be applied to other nucleic-acid-processing motor enzymes.

Indexed as

Translocation, GeneticAdenosine TriphosphateDNADNA HelicasesDNA, Single-StrandedHydrolysisKineticsNanoporesThermococcusAdenosine TriphosphateDNADNA HelicasesDNA, Single-Stranded

Identifiers

PMID30649515
PMCPMC6412116
OpenAlexW2910423220

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
Read underepoch 390

Registered trials

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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.