Evidence map›Paper›PMID 18474528›Full record

ArticleNucleic acids research2008

Mechanism of high-mobility group protein B enhancement of progesterone receptor sequence-specific DNA binding.

Sarah C Roemer, James Adelman, Mair E A Churchill, Dean P Edwards

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.7field-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

20 citing papers in PubMed, 29 citations in OpenAlex.

  1. Article
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  5. Two high-mobility group box domains act together to underwind and kink DNA.Acta crystallographica. Section D, Biological crystallography · 2015
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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.

Sarah C RoemerProgram in Molecular Biology, University of Colorado Denver, School of Medicine, Aurora, CO 80045, USA.
James Adelman
Mair E A Churchill
Dean P Edwards
Baylor College of Medicine · USUniversity of Colorado Denver · US

Funding

PROGESTERONE RECEPTOR INTERACTIONR01CA046938 · NCI · UNIVERSITY OF COLORADO DENVER · PI EDWARDS, DEAN P · 1988 to 2013
$3.3M
STRUCTURAL STUDIES OF CHROMOSOMAL PROTEIN/DNA COMPLEXESR01GM059456 · NIGMS · UNIVERSITY OF COLORADO DENVER · PI CHURCHILL, MAIR E · 1998 to 2002
$468k
NCI NIH HHS CA46938NCI NIH HHS R01 CA046938NIGMS NIH HHS R01 GM059456
6 · The paper itself

Abstract

The DNA-binding domain (DBD) of progesterone receptor (PR) is bipartite containing a zinc module core that interacts with progesterone response elements (PRE), and a short flexible carboxyl terminal extension (CTE) that interacts with the minor groove flanking the PRE. The chromosomal high-mobility group B proteins (HMGB), defined as DNA architectural proteins capable of bending DNA, also function as auxiliary factors that increase the DNA-binding affinity of PR and other steroid receptors by mechanisms that are not well defined. Here we show that the CTE of PR contains a specific binding site for HMGB that is required for stimulation of PR-PRE binding, whereas the DNA architectural properties of HMGB are dispensable. Specific PRE DNA inhibited HMGB binding to the CTE, indicating that DNA and HMGB-CTE interactions are mutually exclusive. Exogenous CTE peptide increased PR-binding affinity for PRE as did deletion of the CTE. In a PR-binding site selection assay, A/T sequences flanking the PRE were enriched by HMGB, indicating that PR DNA-binding specificity is also altered by HMGB. We conclude that a transient HMGB-CTE interaction alters a repressive conformation of the flexible CTE enabling it to bind to preferred sequences flanking the PRE.

Indexed as

Response ElementsAdenineAnimalsBase SequenceBinding SitesChlorocebus aethiopsCOS CellsDNAHMGB ProteinsPeptidesProtein BindingReceptors, ProgesteroneThymineAdenineDNAHMGB ProteinsPeptidesReceptors, ProgesteroneThymine

Identifiers

PMID18474528
PMCPMC2441811
OpenAlexW2055383533

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.