ArticleJournal of molecular biology2008
Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha.
Article in Journal of molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed.
- Genome-wide identification and characteristic analysis of ETS gene family in blood clam Tegillarca granosa.BMC genomics · 2023Article
- Article
- Histone posttranslational modifications and cell fate determination: lens induction requires the lysine acetyltransferases CBP and p300.Nucleic acids research · 2013Article
- Targeting tetramer-forming GABPβ isoforms impairs self-renewal of hematopoietic and leukemic stem cells.Cell stem cell · 2012Article
- Article
- Genomic and biochemical insights into the specificity of ETS transcription factors.Annual review of biochemistry · 2011Review
- Ras signaling requires dynamic properties of Ets1 for phosphorylation-enhanced binding to coactivator CBP.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Methylation-sensitive regulation of TMS1/ASC by the Ets factor, GA-binding protein-alpha.The Journal of biological chemistry · 2009Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Using NMR spectroscopy, we identified and characterized a previously unrecognized structured domain near the N-terminus (residues 35-121) of the ETS family transcription factor GABP alpha. The monomeric domain folds as a five-stranded beta-sheet crossed by a distorted helix. Although globally resembling ubiquitin, the GABP alpha fragment differs in its secondary structure topology and thus appears to represent a new protein fold that we term the OST (On-SighT) domain. The surface of the GABP alpha OST domain contains two predominant clusters of negatively-charged residues suggestive of electrostatically driven interactions with positively-charged partner proteins. Following a best-candidate approach to identify such a partner, we demonstrated through NMR-monitored titrations and glutathione S-transferase pulldown assays that the OST domain binds to the CH1 and CH3 domains of the co-activator histone acetyltransferase CBP/p300. This provides a direct structural link between GABP and a central component of the transcriptional machinery.
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Registered trials
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