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Published online before print June 28, 2007
Protein Science, DOI: 10.1110/ps.072792007
 Copyright © 2007 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of the general transcription factor 2I domain in mouse TFII-I protein

Yukiko Doi-Katayama1,4, Fumiaki Hayashi1, Makoto Inoue1, Takashi Yabuki1, Masaaki Aoki1, Eiko Seki1, Takayoshi Matsuda1, Takanori Kigawa1, Mayumi Yoshida1, Mikako Shirouzu1, Takaho Terada1, Yoshihide Hayashizaki1, Shigeyuki Yokoyama1,2, and Hiroshi Hirota1,3

1 RIKEN Genomic Sciences Center, Tsurumi-ku, Yokohama 230-0045, Japan
2 Graduate School of Science, The University of Tokyo, Tokyo 113-0033, Japan
3 Graduate School, Yokohama City University, Tsurumi-ku, Yokohama 230-0045, Japan

(RECEIVED January 25, 2007; FINAL REVISION May 1, 2007; ACCEPTED May 3, 2007)

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.

Keywords: GTF2I domain; transcription factor; nuclear magnetic resonance; protein structure

4 Present address: Nikon Corporation, Shinagawa, Tokyo, Japan.

Supplemental material: see www.proteinscience.org

Reprint requests to: Hiroshi Hirota, RIKEN Genomic Sciences Center, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan; e-mail: hirota{at}gsc.riken.jp; fax: 81-45-503-9210.

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.072792007.


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Copyright © 2007 by The Protein Society.