Solution structure of the general transcription factor 2I domain in mouse TFII-I protein
Solution structure of the general transcription factor 2I domain in mouse TFII-I protein
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DOI：
10.1110/ps.072792007
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发表时间：
2007-08-01
期刊：
影响因子：
8
通讯作者：
Hirota, Hiroshi
中科院分区：
文献类型：
--
作者：
Doi-Katayama, Yukiko;Hayashi, Fumiaki;Hirota, Hiroshi
通用转录因子TFII-I，与相应的基因名称GTF 2 I，是一种不寻常的转录调节因子，与基础和信号诱导的转录因子。TFII-I由六个GTF 2 I重复结构域组成，称为I-重复R1-R6。GTF 2 I结构域的结构和功能尚不清楚，尽管其含有螺旋-环-螺旋基序，基于生物化学分析，其被认为是蛋白质-蛋白质相互作用区域。在这里，我们报告的解决方案结构的第五个重复的六个GTF 2 I重复结构域从鼠TFII-I，这是确定的异频多维NMR光谱（PDB代码1 Q60）。GTF 2 I结构域的三维结构被分类为新折叠，由四个螺旋（残基8-24、34-39、63-71和83-91）、两个反平行β链（残基44-47和77-80）和在片层1和螺旋3之间含有两个β转角的明确定义的环组成。所有的重复序列可能具有与重复序列5相似的折叠，因为GTF 2 I重复序列结构域中的保守残基组装在疏水核心、转角和二级结构元件上，如TFII-I中第一至第六个GTF 2 I重复序列的序列比较所揭示的.
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.