Evidence map›Paper›PMID 25902201›Full record

ArticleJournal of molecular biology2015

E. coli Gyrase Fails to Negatively Supercoil Diaminopurine-Substituted DNA.

Mónica Fernández-Sierra, Qing Shao, Chandler Fountain, Laura Finzi, David Dunlap

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 15 citations in OpenAlex.

  1. MACRO-MOLECULAR CROWDING FAVORS WRITHE IN UNWOUND DNA.bioRxiv : the preprint server for biology · 2026
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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

5 authors at 1 institution in 1 country.

Mónica Fernández-SierraDepartments of Physics and Cell Biology, Emory University, Atlanta, GA 30322, USA.
Qing ShaoDepartments of Physics and Cell Biology, Emory University, Atlanta, GA 30322, USA.
Chandler FountainDepartments of Physics and Cell Biology, Emory University, Atlanta, GA 30322, USA.
Laura FinziDepartments of Physics and Cell Biology, Emory University, Atlanta, GA 30322, USA.
David DunlapDepartments of Physics and Cell Biology, Emory University, Atlanta, GA 30322, USA. Electronic address: ddunlap@emory.edu.
Emory University · US

Funding

The lambda bacteriophage regulatory loopR01GM084070 · NIGMS · EMORY UNIVERSITY · PI FINZI, LAURA · 2009 to 2021
$4.1M
NIGMS NIH HHS R01 GM084070PHS HHS RGM084070A
6 · The paper itself

Abstract

Type II topoisomerases modify DNA supercoiling, and crystal structures suggest that they sharply bend DNA in the process. Bacterial gyrases are a class of type II topoisomerases that can introduce negative supercoiling by creating a wrap of DNA before strand passage. Isoforms of these essential enzymes were compared to reveal whether they can bend or wrap artificially stiffened DNA. Escherichia coli gyrase and human topoisomerase IIα were challenged with normal DNA or stiffer DNA produced by polymerase chain reaction reactions in which diaminopurine (DAP) replaced adenine deoxyribonucleotide triphosphates. On single DNA molecules twisted with magnetic tweezers to create plectonemes, the rates or pauses during relaxation of positive supercoils in DAP-substituted versus normal DNA were distinct for both enzymes. Gyrase struggled to bend or perhaps open a gap in DAP-substituted DNA, and segments of wider DAP DNA may have fit poorly into the N-gate of the human topoisomerase IIα. Pauses during processive activity on both types of DNA exhibited ATP dependence consistent with two pathways leading to the strand-passage-competent state with a bent gate segment and a transfer segment trapped by an ATP-loaded and latched N-gate. However, E. coli DNA gyrase essentially failed to negatively supercoil 35% stiffer DAP DNA.

Indexed as

2-AminopurineAdenosine TriphosphateAntigens, NeoplasmDNA-Binding ProteinsDNA GyraseDNA, SuperhelicalDNA Topoisomerases, Type IIElectrophoretic Mobility Shift AssayEscherichia coli ProteinsNucleic Acid ConformationProtein ConformationSalmonella2-AminopurineAdenosine TriphosphateAntigens, NeoplasmDNA-Binding ProteinsDNA GyraseDNA, SuperhelicalDNA Topoisomerases, Type IIEscherichia coli ProteinsdiaminopurineDNA wrappinggyrasenegative supercoilingtopoisomerase

Identifiers

PMID25902201
PMCPMC4457584
OpenAlexW1964037253

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.