Evidence map›Paper›PMID 19236006›Full record

ArticleBiochemistry2009

Enhancement of DNA flexibility in vitro and in vivo by HMGB box A proteins carrying box B residues.

Nadia T Sebastian, Emily M Bystry, Nicole A Becker, L James Maher

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

18 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Article
  3. High-Resolution Characterization of DNA/Protein Complexes in Living Bacteria.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. High-resolution mapping of architectural DNA binding protein facilitation of a DNA repression loop in Escherichia coli.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Gene repression by minimal lac loops in vivo.Nucleic acids research · 2010
    Article
  16. Article
  17. DNA curvature and flexibility in vitro and in vivo.Quarterly reviews of biophysics · 2010
    Review
  18. Review
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

4 authors at 2 institutions in 1 country.

Nadia T SebastianDepartment of Chemistry, Creighton University, 2500 California Place, Omaha, Nebraska 68178, USA.
Emily M Bystry
Nicole A Becker
L James Maher
Mayo Clinic · USCreighton University · US

Funding

Enhancement of Cellular DNA FlexibilityR01GM075965 · NIGMS · MAYO CLINIC ROCHESTER · PI MAHER, LOUIS JAMES · 2006 to 2018
$4.2M
NIGMS NIH HHS GM 75965NIGMS NIH HHS R01 GM075965
6 · The paper itself

Abstract

HMGB proteins are abundant non-histone components of eukaryotic chromatin. The biological function of DNA sequence-nonspecific HMGB proteins is obscure. These proteins are composed of one or two conserved HMG box domains, each forming three alpha-helices that fold into a sequence-nonspecific DNA-binding module recognizing the DNA minor groove. Box A and box B homology domains have subtle sequence differences such that box B domains bend DNA strongly while DNA bending by isolated box A domains is weaker. Both box A and box B domains preferentially bind to distorted DNA structures. Here we show using DNA cyclization kinetics assays in vitro and Escherichia coli DNA looping assays in vivo that an isolated HMG box A domain derived from human HMGB2 folds poorly and does not enhance apparent DNA flexibility. Surprisingly, substitution of a small number of cationic residues from the N-terminal leader of a functional yeast box B protein, Nhp6Ap, confers the ability to enhance DNA flexibility. These results demonstrate important roles for cationic leader amino acids in HMGB folding, DNA interaction, and DNA bending.

Indexed as

Nucleic Acid ConformationCircular DichroismDNADNA-Binding ProteinsEscherichia coliEscherichia coli ProteinsFluorescence PolarizationHMGB2 ProteinHMG-Box DomainsHMGB ProteinsHMGN ProteinsHumansLac OperonPeptide FragmentsProtein BindingProtein Sorting SignalsDNADNA-Binding ProteinsEscherichia coli ProteinsHMGB2 ProteinHMGB ProteinsHMGN Proteinshns protein, E coliNHP6A protein, S cerevisiaePeptide FragmentsProtein Sorting SignalsRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID19236006
PMCPMC2668924
OpenAlexW2142810985

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.