| Title | Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha |
| Publication Type | Journal Article |
| Year of Publication | 2008 |
| Authors | Kang, HS, Nelson, ML, Mackereth, CD, Scharpf, M, Graves, BJ, McIntosh, LP |
| Journal | Journal of Molecular Biology |
| Volume | 377 |
| Pagination | 636-646 |
| Date Published | Mar |
| Type of Article | Article |
| ISBN Number | 0022-2836 |
| Keywords | BACKBONE DYNAMICS, C-13-LABELED PROTEINS, CREB-BINDING-PROTEIN, ESCHERICHIA-COLI, HIGH-RESOLUTION, HYPOXIA-INDUCIBLE FACTOR-1-ALPHA, LARGER PROTEINS, NEUROMUSCULAR-JUNCTION, NMR, NMR EXPERIMENTS, protein-protein interaction, RESIDUAL DIPOLAR COUPLINGS, SPECTROSCOPY, TRANSCRIPTION FACTOR, UBIQUITIN |
| 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(x 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. (C) 2008 Elsevier Ltd. All rights reserved. |
| URL | <Go to ISI>://000255374200006 |
