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  • The EMBO Journal (2000) 19, 1346 - 1356
  • doi:10.1093/emboj/19.6.1346

Structure of the central core domain of TFIIEbold beta with a novel double-stranded DNA-binding surface

Masahiko Okuda1, Yoshinori Watanabe2, Hideyasu Okamura1, Fumio Hanaoka2, Yoshiaki Ohkuma2 and Yoshifumi Nishimura1,3

  1. Graduate School of Integrated Science, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama 236-0027, Japan
  2. Institute for Molecular and Cellular Biology, Osaka University, 1-3 Yamada-oka, Suita, Osaka 565-0871 Japan
  3. Genomic Sciences Center (GSC), RIKEN (The Institute of Physical and Chemical Research), 2-1 Hirosawa, Wako-shi, Saitama 351-0198, Japan

Correspondence to:

Yoshifumi Nishimura, E-mail: nisimura@yokohama-cu.ac.jp

Received 16 August 1999; Accepted 27 January 2000; Revised 8 November 1999

Human general transcription factor TFIIE consists of two subunits, TFIIEalpha and TFIIEbeta. Recently, TFIIEbeta has been found to bind to the region where the promoter starts to open to be single-stranded upon transcription initiation by RNA polymerase II. Here, the central core domain of human TFIIEbeta (TFIIEbetac) has been identified by a limited proteolysis. This solution structure has been determined by NMR. It consists of three helices with a beta hairpin at the C–terminus, resembling the winged helix proteins. However, TFIIEbetac shows a novel double-stranded DNA-binding activity where the DNA-binding surface locates on the opposite side to the previously reported winged helix motif by forming a positively charged furrow. A model will be proposed that TFIIE stabilizes the preinitiation complex by binding not only to the general transcription factors together with RNA polymerase II but also to the promoter DNA, where double-stranded DNA starts to open to be single-stranded upon activation of the preinitiation complex.

  • Keywords:

    • DNA-binding,
    • general transcription factor,
    • NMR,
    • TFIIE,
    • winged helix