ArticleProtein science : a publication of the Protein Society2007
Solution structure of the general transcription factor 2I domain in mouse TFII-I protein.
Article in Protein science : a publication of the Protein Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed.
- Canine hyper-sociability structural variants associated with altered three-dimensional chromatin state.BMC genomics · 2024Article
- Regulation of RNA Polymerase II Transcription Initiation and Elongation by Transcription Factor TFII-I.Frontiers in molecular biosciences · 2021Review
- TFII-I/Gtf2i and Erythro-Megakaryopoiesis.Frontiers in physiology · 2020Article
- Functional interrelationship between TFII-I and E2F transcription factors at specific cell cycle gene loci.Journal of cellular biochemistry · 2018Article
- Pathophysiology of TFII-I: Old Guard Wearing New Hats.Trends in molecular medicine · 2017Review
- A specific missense mutation in GTF2I occurs at high frequency in thymic epithelial tumors.Nature genetics · 2014Article
- Genomic and proteomic analysis of transcription factor TFII-I reveals insight into the response to cellular stress.Nucleic acids research · 2014Article
- Evolution of general transcription factors.Journal of molecular evolution · 2013Article
- GTF2IRD2 from the Williams-Beuren critical region encodes a mobile-element-derived fusion protein that antagonizes the action of its related family members.Journal of cell science · 2012Article
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14 authors.
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Abstract
The general transcription factor TFII-I, with the corresponding gene name GTF2I, is an unusual transcriptional regulator that associates with both basal and signal-induced transcription factors. TFII-I consists of six GTF2I repeat domains, called I-repeats R1-R6. The structure and function of the GTF2I domain are not clearly understood, even though it contains a helix-loop-helix motif, which is considered to be the protein-protein interaction area, based on biochemical analyses. Here, we report the solution structure of the fifth repeat of the six GTF2I repeat domains from murine TFII-I, which was determined by heteronuclear multidimensional NMR spectroscopy (PDB code 1Q60). The three-dimensional structure of the GTF2I domain is classified as a new fold, consisting of four helices (residues 8-24, 34-39, 63-71, and 83-91), two antiparallel beta strands (residues 44-47 and 77-80), and a well-defined loop containing two beta-turns between sheet 1 and helix 3. All of the repeats probably have similar folds to that of repeat 5, because the conserved residues in the GTF2I repeat domains are assembled on the hydrophobic core, turns, and secondary structure elements, as revealed by a comparison of the sequences of the first through the sixth GTF2I repeats in TFII-I.
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