Evidence map›Paper›PMID 23661683›Full record

ArticleNucleic acids research2013

Control of DNA minor groove width and Fis protein binding by the purine 2-amino group.

Stephen P Hancock, Tahereh Ghane, Duilio Cascio, Remo Rohs, Rosa Di Felice, Reid C Johnson

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
5.4field-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

54 citing papers in PubMed, 88 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. SynonymousNAR genomics and bioinformatics · 2024
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Energy Landscapes for Base-Flipping in a Model DNA Duplex.The journal of physical chemistry. B · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Crystal structure of the nucleoid-associated protein Fis (PA4853) from Pseudomonas aeruginosa.Acta crystallographica. Section F, Structural biology communications · 2020
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  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

6 authors at 2 institutions in 1 country.

Stephen P HancockDepartment of Biological Chemistry, David Geffen School of Medicine at the University of California at Los Angeles, Los Angeles, CA 90095-1737, USA.
Tahereh Ghane
Duilio Cascio
Remo Rohs
Rosa Di Felice
Reid C Johnson
University of California, Los Angeles · USUniversity of Southern California · US

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Molecular Analysis of Site Specific DNA RecombinationR37GM038509 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI JOHNSON, REID C · 2005 to 2014
$6.6M
MOLECULAR ANALYSIS OF SITE-SPECIFIC DNA RECOMBINATIONR01GM038509 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI JOHNSON, REID C · 1987 to 2018
$4.7M
NCRR NIH HHS 5P41RR015301-10NIGMS NIH HHS GM038509NIGMS NIH HHS P41 GM103403-10NIGMS NIH HHS R37 GM038509
6 · The paper itself

Abstract

The width of the DNA minor groove varies with sequence and can be a major determinant of DNA shape recognition by proteins. For example, the minor groove within the center of the Fis-DNA complex narrows to about half the mean minor groove width of canonical B-form DNA to fit onto the protein surface. G/C base pairs within this segment, which is not contacted by the Fis protein, reduce binding affinities up to 2000-fold over A/T-rich sequences. We show here through multiple X-ray structures and binding properties of Fis-DNA complexes containing base analogs that the 2-amino group on guanine is the primary molecular determinant controlling minor groove widths. Molecular dynamics simulations of free-DNA targets with canonical and modified bases further demonstrate that sequence-dependent narrowing of minor groove widths is modulated almost entirely by the presence of purine 2-amino groups. We also provide evidence that protein-mediated phosphate neutralization facilitates minor groove compression and is particularly important for binding to non-optimally shaped DNA duplexes.

Indexed as

Base PairingDNAFactor For Inversion Stimulation ProteinMolecular Dynamics SimulationNucleic Acid ConformationPhosphatesProtein BindingPurinesDNAFactor For Inversion Stimulation ProteinPhosphatesPurines

Identifiers

PMID23661683
PMCPMC3711457
OpenAlexW2117314105

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.