Evidence map›Paper›PMID 29662209›Full record

ArticleNature chemical biology2018

Dynamic coupling between conformations and nucleotide states in DNA gyrase.

Aakash Basu, Matthew Hobson, Paul Lebel, Louis E Fernandes, Elsa M Tretter, James M Berger, Zev Bryant

Abstract read
In one paragraph

Article in Nature chemical biology, 2018. 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
–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

13 citing papers in PubMed.

  1. Article
  2. Structural basis of chiral wrap and T-segment capture byProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Deciphering the mechanical code of the genome and epigenome.Nature structural & molecular biology · 2022
    Article
  8. Article
  9. Direct observation of helicase-topoisomerase coupling within reverse gyrase.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  10. Cas9 interrogates DNA in discrete steps modulated by mismatches and supercoiling.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. 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

7 authors.

Aakash BasuDepartment of Applied Physics, Stanford University, Stanford, CA, USA.
Matthew HobsonDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Paul LebelDepartment of Applied Physics, Stanford University, Stanford, CA, USA.
Louis E FernandesDepartment of Bioengineering, Stanford University, Stanford, CA, USA.
Elsa M TretterDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA, USA.
James M BergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Zev BryantDepartment of Bioengineering, Stanford University, Stanford, CA, USA. zevry@stanford.edu.

Funding

PROGRAM IN MOLECULAR BIOPHYSICST32GM008403 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BARRICK, DOUGLAS E. · 1990 to 2019
$13.5M
Structural and Biochemical Analyses of Type II DNA TopoisomerasesR01CA077373 · NCI · UNIVERSITY OF CALIFORNIA BERKELEY · PI BERGER, JAMES M. · 1999 to 2021
$7.6M
Structural Dynamics and Mechanochemical Coupling in Nucleoprotein MachinesR01GM106159 · NIGMS · STANFORD UNIVERSITY · PI Zev Bryant · 2014 to 2026
$3.2M
NCI NIH HHS R01 CA077373NIGMS NIH HHS R01 GM106159NIGMS NIH HHS T32 GM008403
6 · The paper itself

Abstract

Gyrase is an essential bacterial molecular motor that supercoils DNA using a conformational cycle in which chiral wrapping of > 100 base pairs confers directionality on topoisomerization. To understand the mechanism of this nucleoprotein machine, global structural transitions must be mapped onto the nucleotide cycle of ATP binding, hydrolysis and product release. Here we investigate coupling mechanisms using single-molecule tracking of DNA rotation and contraction during Escherichia coli gyrase activity under varying nucleotide conditions. We find that ADP must be exchanged for ATP to drive the rate-limiting remodeling transition that generates the chiral wrap. ATP hydrolysis accelerates subsequent duplex strand passage and is required for resetting the enzyme and recapturing transiently released DNA. Our measurements suggest how gyrase coordinates DNA rearrangements with the dynamics of its ATP-driven protein gate, how the motor minimizes futile cycles of ATP hydrolysis and how gyrase may respond to changing cellular energy levels to link gene expression with metabolism.

Indexed as

Adenosine DiphosphateAdenosine TriphosphateDNADNA GyraseEscherichia coliGene Expression ProfilingGene Expression RegulationHydrolysisKineticsModels, MolecularNucleic Acid ConformationNucleotidesProtein BindingProtein ConformationStereoisomerismAdenosine DiphosphateAdenosine TriphosphateDNADNA GyraseNucleotides

Identifiers

PMID29662209
PMCPMC10121156

What OpenQuestion holds

Textmetadata
LicenceTDM
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.