Evidence map›Paper›PMID 10825199›Full record

ArticleMolecular and cellular biology2000

Mechanism for specificity by HMG-1 in enhanceosome assembly.

K B Ellwood, Y M Yen, R C Johnson, M Carey

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
  2. Journal of virology · 2021
    Article
  3. Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. HMGB1 in health and disease.Molecular aspects of medicine · 2014
    Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. HMBG1 mediates ischemia-reperfusion injury by TRIF-adaptor independent Toll-like receptor 4 signaling.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2011
    Article
  18. Review
  19. High-mobility group protein box-1 and its relevance to cerebral ischemia.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2010
    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

4 authors at 1 institution in 1 country.

K B EllwoodDepartment of Biological Chemistry, University of California at Los Angeles School of Medicine, Los Angeles, California 90095-1737, USA.
Y M Yen
R C Johnson
M 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

Assembly of enhanceosomes requires architectural proteins to facilitate the DNA conformational changes accompanying cooperative binding of activators to a regulatory sequence. The architectural protein HMG-1 has been proposed to bind DNA in a sequence-independent manner, yet, paradoxically, it facilitates specific DNA binding reactions in vitro. To investigate the mechanism of specificity we explored the effect of HMG-1 on binding of the Epstein-Barr virus activator ZEBRA to a natural responsive promoter in vitro. DNase I footprinting, mutagenesis, and electrophoretic mobility shift assay reveal that HMG-1 binds cooperatively with ZEBRA to a specific DNA sequence between two adjacent ZEBRA recognition sites. This binding requires a strict alignment between two adjacent ZEBRA sites and both HMG boxes of HMG-1. Our study provides the first demonstration of sequence-dependent binding by a nonspecific HMG-box protein. We hypothesize how a ubiquitous, nonspecific architectural protein can function in a specific context through the use of rudimentary sequence recognition coupled with cooperativity. The observation that an abundant architectural protein can bind DNA cooperatively and specifically has implications towards understanding HMG-1's role in mediating DNA transactions in a variety of enzymological systems.

Indexed as

Gene Expression RegulationAnimalsCarrier ProteinsDNAHigh Mobility Group ProteinsHMGB1 ProteinMutationNucleic Acid ConformationNucleoproteinsPromoter Regions, GeneticRecombinant ProteinsCarrier ProteinsDNAHigh Mobility Group ProteinsHMGB1 ProteinNucleoproteinsRecombinant Proteins

Identifiers

PMID10825199
PMCPMC85803
OpenAlexW2090213064

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.