Evidence map›Paper›PMID 17097674›Full record

ArticleJournal of molecular biology2007

Structure-based analysis of HU-DNA binding.

Kerren K Swinger, Phoebe A Rice

Abstract read
In one paragraph

Article in Journal of molecular biology, 2007. 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
–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

54 citing papers in PubMed.

  1. Pangenomics insights of enterococcus faecium human isolates and identification of novel therapeutic targets by in silico subtractive genomics.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2026
    Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. NFrontiers in microbiology · 2024
    Article
  7. Review
  8. Article
  9. Antimicrobial resistance and mechanisms of epigenetic regulation.Frontiers in cellular and infection microbiology · 2023
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. The structural basis of African swine fever virus pA104R binding to DNA and its inhibition by stilbene derivatives.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  18. 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

2 authors.

Kerren K SwingerDepartment of Biochemistry and Molecular Biology, University of Chicago, 920 E 58th Street, Chicago, IL 60637, USA.
Phoebe A Rice

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Understanding DNA specificity in the IHF/HU familyR01GM066011 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 2002 to 2005
$1.0M
Structural Biology of a Serine DNA RecombinaseR56GM066011 · NIGMS · UNIVERSITY OF CHICAGO · PI RICE, PHOEBE A · 2007 to 2007
$261k
NIGMS NIH HHS GM66011NIGMS NIH HHS R01 GM066011NIGMS NIH HHS R56 GM066011NIGMS NIH HHS T32 GM007183NIGMS NIH HHS T32 GM07183H
6 · The paper itself

Abstract

HU and IHF are prokaryotic proteins that induce very large bends in DNA. They are present in high concentrations in the bacterial nucleoid and aid in chromosomal compaction. They also function as regulatory cofactors in many processes, such as site-specific recombination and the initiation of replication and transcription. HU and IHF have become paradigms for understanding DNA bending and indirect readout of sequence. While IHF shows significant sequence specificity, HU binds preferentially to certain damaged or distorted DNAs. However, none of the structurally diverse HU substrates previously studied in vitro is identical with the distorted substrates in the recently published Anabaena HU(AHU)-DNA cocrystal structures. Here, we report binding affinities for AHU and the DNA in the cocrystal structures. The binding free energies for formation of these AHU-DNA complexes range from approximately 10-14.5 kcal/mol, representing K(d) values in the nanomolar to low picomolar range, and a maximum stabilization of at least approximately 6.3 kcal/mol relative to complexes with undistorted, non-specific DNA. We investigated IHF binding and found that appropriate structural distortions can greatly enhance its affinity. On the basis of the coupling of structural and relevant binding data, we estimate the amount of conformational strain in an IHF-mediated DNA kink that is relieved by a nick (at least 0.76 kcal/mol) and pinpoint the location of the strain. We show that AHU has a sequence preference for an A+T-rich region in the center of its DNA-binding site, correlating with an unusually narrow minor groove. This is similar to sequence preferences shown by the eukaryotic nucleosome.

Indexed as

AnabaenaBacterial ProteinsBase SequenceBinding SitesCrystallography, X-RayDNADNA-Binding ProteinsDose-Response Relationship, DrugEscherichia coliIntegration Host FactorsModels, MolecularMolecular ConformationMolecular Sequence DataNucleosomesProtein BindingTranscription, GeneticBacterial ProteinsDNADNA-Binding Proteinshistone-like protein HU, bacteriaIntegration Host FactorsNucleosomes

Identifiers

PMID17097674
PMCPMC1945228

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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.