Structural insights into the asymmetric effects of zinc-ligand cysteine mutations in the novel zinc ribbon domain of human TFIIEα for transcription

Masahiko Okuda, Aki Tanaka, Fumio Hanaoka, Yoshiaki Ohkuma, Yoshifumi Nishimura*

*この論文の責任著者

研究成果: ジャーナルへの寄稿学術論文査読

5 被引用数 (Scopus)

抄録

The large subunit of TFIIE (TFIIEα) has a highly conserved zinc ribbon domain, which is essential for transcription. Recently, we determined the solution structure of this domain to be that of a novel zinc finger motif [Okuda et al. (2004) J. Biol. Chem. 279, 51395-51403]. On examination of the functions of four cysteine mutants of TFIIEα, in which each of four zinc-liganded cysteines was replaced by alanine, we found an interesting functional asymmetry; on a supercoiled template, the two C-terminal mutants did not show any transcriptional activity, however, the two N-terminal mutants retained about 20% activity. Furthermore, these two pairs of mutants showed distinct binding abilities as to several general transcription factors. To obtain structural insights into the asymmetry, here we have analyzed the structures of the four cysteine mutants of the zinc ribbon domain by CD and NMR. All four mutants possessed a characteristic partially folded structure coordinating with a zinc atom, despite the imperfect set of cysteine-ligands. However, they equilibrated with several structures including the random coil structure. Unexpectedly, the two N-terminal mutants mainly equilibrated with the random coil structure, while the two C-terminal ones mainly equilibrated with folded structures. The characteristic structure formation of each mutant was reversible, which totally depended on the zinc binding.

本文言語英語
ページ(範囲)443-449
ページ数7
ジャーナルJournal of Biochemistry
138
4
DOI
出版ステータス出版済み - 2005/10

ASJC Scopus 主題領域

  • 生化学
  • 分子生物学

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