Evidence map›Paper›PMID 12771212›Full record

ArticleNucleic acids research2003

The role of intercalating residues in chromosomal high-mobility-group protein DNA binding, bending and specificity.

Janet Klass, Frank V Murphy, Susan Fouts, Melissa Serenil, Anita Changela, Jessica Siple, Mair E A Churchill

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

30 citing papers in PubMed, 68 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Structure and Functions of HMGB2 Protein.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. Review
  9. Two high-mobility group box domains act together to underwind and kink DNA.Acta crystallographica. Section D, Biological crystallography · 2015
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Crystal structure of QscR, a Pseudomonas aeruginosa quorum sensing signal receptor.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  16. Article
  17. Article
  18. Review
  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

7 authors at 1 institution in 1 country.

Janet KlassDepartment of Pharmacology, The University of Colorado Health Sciences Center, 4200 East Ninth Avenue, Denver, CO 80262, USA.
Frank V Murphy
Susan Fouts
Melissa Serenil
Anita Changela
Jessica Siple
Mair E A Churchill
University of Colorado Health · US

Funding

STRUCTURAL STUDIES OF CHROMOSOMAL PROTEIN/DNA COMPLEXESR01GM059456 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 1998 to 2002
$468k
NIGMS NIH HHS R01 GM059456NIGMS NIH HHS R01-GM59456
6 · The paper itself

Abstract

Ubiquitous high-mobility-group (HMGB) chromosomal proteins bind DNA in a non-sequence- specific fashion to promote chromatin function and gene regulation. Minor groove DNA binding of the HMG domain induces substantial DNA bending toward the major groove, and several interfacial residues contribute by DNA intercalation. The role of the intercalating residues in DNA binding, bending and specificity was systematically examined for a series of mutant Drosophila HMGB (HMG-D) proteins. The primary intercalating residue of HMG-D, Met13, is required both for high-affinity DNA binding and normal DNA bending. Leu9 and Tyr12 directly interact with Met13 and are required for HMG domain stability in addition to linear DNA binding and bending, which is an important function for these residues. In contrast, DNA binding and bending is retained in truncations of intercalating residues Val32 and Thr33 to alanine, but DNA bending is decreased for the glycine substitutions. Furthermore, substitution of the intercalating residues with those predicted to be involved in the specificity of the HMG domain transcription factors results in increased DNA affinity and decreased DNA bending without increased specificity. These studies reveal the importance of residues that buttress intercalating residues and suggest that features of the HMG domain other than a few base-specific hydrogen bonds distinguish the sequence-specific and non-sequence-specific HMG domain functions.

Indexed as

Amino AcidsAmino Acid SequenceAnimalsBinding SitesDNADNA-Binding ProteinsDrosophila ProteinsElectrophoretic Mobility Shift AssayHigh Mobility Group ProteinsModels, MolecularMolecular Sequence DataMutationNucleic Acid ConformationProtein Structure, TertiarySequence AlignmentAmino AcidsDNADNA-Binding ProteinsDrosophila ProteinsHigh Mobility Group Proteins

Identifiers

PMID12771212
PMCPMC156723
OpenAlexW2163422932

What OpenQuestion holds

Textmetadata
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.