Evidence map›Paper›PMID 11058116›Full record

ArticleNucleic acids research2000

Analysis of Groucho-histone interactions suggests mechanistic similarities between Groucho- and Tup1-mediated repression.

R D Flores-Saaib, A J Courey

Open access · bronzeAbstract read
In one paragraph

Article in Nucleic acids research, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

33 citing papers in PubMed, 48 citations in OpenAlex.

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  16. Dynamic expression of Groucho-related genes Grg1 and Grg3 in foregut endoderm and antagonism of differentiation.Developmental dynamics : an official publication of the American Association of Anatomists · 2010
    Article
  17. Groucho corepressor functions as a cofactor for the Knirps short-range transcriptional repressor.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
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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

2 authors at 1 institution in 1 country.

R D Flores-SaaibDepartment of Chemistry and Biochemistry, 5034 Young Hall, University of California, Los Angeles, 405 Hilgard Avenue, Los Angeles, CA 90095, USA.
A J Courey
University of California, Los Angeles · US

Funding

Repressor/co-repressor oligomerization and developmentR01GM044522 · NIGMS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI COUREY, ALBERT J · 1990 to 2011
$4.1M
NIGMS NIH HHS GM44522NIGMS NIH HHS R01 GM044522
6 · The paper itself

Abstract

The Drosophila Groucho (Gro) protein is the defining member of a family of metazoan corepressors that have roles in many aspects of development, including segmentation, dorsal/ventral pattern formation, Notch signaling, and Wnt/Wg signaling. Previous speculation has suggested that Gro may be orthologous to the yeast corepressor Tup1. In support of this idea, a detailed alignment between the C-terminal WD-repeat domains of these two proteins shows that each Gro WD repeat is most similar to the Tup1 WD repeat occupying the corresponding position in that protein. Our analysis of Gro-histone interactions provides further support for a close evolutionary relationship between Gro and Tup1. In particular, we show that, as with the N-terminal region of Tup1, the N-terminal region of Gro is necessary and sufficient for direct binding to histones. The highest affinity interaction is with histone H3 and binding is primarily observed with hypoacetylated histones. Using transient transfection assays, we show that a Gal4-Gro fusion protein containing the histone-binding domain is able to repress transcription. Deletions that weaken histone binding also weaken repression. These findings, along with our recent report that Gro interacts with the histone deacetylase Rpd3, suggest a mechanism for Gro-mediated repression.

Indexed as

Drosophila melanogasterNuclear ProteinsSaccharomyces cerevisiae ProteinsAcetylationAmino Acid SequenceAnimalsBasic Helix-Loop-Helix ProteinsCell LineDNA-Binding ProteinsDown-RegulationFungal ProteinsHistone DeacetylasesHistonesMolecular Sequence DataProtein BindingProtein Structure, TertiaryBasic Helix-Loop-Helix ProteinsDNA-Binding ProteinsFungal Proteinsgro protein, DrosophilaHistone DeacetylasesHistonesNuclear ProteinsRecombinant Fusion ProteinsRepressor ProteinsSaccharomyces cerevisiae ProteinsTUP1 protein, S cerevisiae

Identifiers

PMID11058116
PMCPMC113153
OpenAlexW2023014998

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.