Evidence map›Paper›PMID 12024049›Full record

ArticleMolecular and cellular biology2002

The DNA architectural protein HMGB1 displays two distinct modes of action that promote enhanceosome assembly.

Katherine Mitsouras, Ben Wong, Charina Arayata, Reid C Johnson, Michael Carey

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

40 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Structure and Functions of HMGB2 Protein.International journal of molecular sciences · 2023
    Review
  3. Review
  4. Journal of virology · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  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

5 authors at 1 institution in 1 country.

Katherine MitsourasDepartment of Biological Chemistry, UCLA School of Medicine, Los Angeles, California 90095-1737, USA.
Ben Wong
Charina Arayata
Reid C Johnson
Michael Carey
University of California, Los Angeles · US

Funding

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
Mechanisms of Synergistic Gene Activation by ZEBRAR01GM057283 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI CAREY, MICHAEL F · 1998 to 2005
$1.4M
NIGMS NIH HHS GM057283NIGMS NIH HHS GM38509NIGMS NIH HHS R01 GM038509NIGMS NIH HHS R01 GM057283NIGMS NIH HHS R37 GM038509
6 · The paper itself

Abstract

HMGB1 (also called HMG-1) is a DNA-bending protein that augments the affinity of diverse regulatory proteins for their DNA sites. Previous studies have argued for a specific interaction between HMGB1 and target proteins, which leads to cooperative binding of the complex to DNA. Here we propose a different model that emerged from studying how HMGB1 stimulates enhanceosome formation by the Epstein-Barr viral activator Rta on a target gene, BHLF-1. HMGB1 stimulates binding of individual Rta dimers to multiple sites in the enhancer. DNase I and hydroxyl radical footprinting, electrophoretic mobility shift assays, and immobilized template assays failed to reveal stable binding of HMGB1 within the complex. Furthermore, mutational analysis failed to identify a specific HMGB1 target sequence. The effect of HMGB1 on Rta could be reproduced by individual HMG domains, yeast HMO1, or bacterial HU. These results, combined with the effects of single-amino-acid substitutions within the DNA-binding surface of HMGB1 domain A, argue for a mechanism whereby DNA-binding and bending by HMGB1 stimulate Rta-DNA complex formation in the absence of direct interaction with Rta or a specific HMGB1 target sequence. The data contrast with our analysis of HMGB1 action on another BHLF-1 regulatory protein called ZEBRA. We discuss the two distinct modes of HMGB1 action on a single regulatory region and propose how HMGB1 can function in diverse contexts.

Indexed as

Enhancer Elements, GeneticAnimalsBinding SitesCell LineDNADNA-Binding ProteinsDNA FootprintingHMGB1 ProteinHydroxyl RadicalImmediate-Early ProteinsMutationTrans-ActivatorsViral ProteinsBRLF1 protein, Human herpesvirus 4BZLF1 protein, Herpesvirus 4, HumanDNADNA-Binding ProteinsHMGB1 ProteinHydroxyl RadicalImmediate-Early ProteinsTrans-ActivatorsViral Proteins

Identifiers

PMID12024049
PMCPMC133865
OpenAlexW2158668067

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.