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Structural insight into the TFIIE–TFIIH interaction: TFIIE and p53 share the binding region on TFIIH
Author(s) -
Okuda Masahiko,
Tanaka Aki,
Satoh Manami,
Mizuta Shoko,
Takazawa Manabu,
Ohkuma Yoshiaki,
Nishimura Yoshifumi
Publication year - 2008
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2008.47
Subject(s) - transcription factor ii h , transcription factor ii a , transcription preinitiation complex , transcription factor ii e , biology , pleckstrin homology domain , rna polymerase ii holoenzyme , heterotetramer , general transcription factor , microbiology and biotechnology , transcription factor ii b , biophysics , biochemistry , protein subunit , transcription factor , promoter , signal transduction , rna , transcriptional regulation , rna polymerase , gene expression , gene
RNA polymerase II and general transcription factors (GTFs) assemble on a promoter to form a transcription preinitiation complex (PIC). Among the GTFs, TFIIE recruits TFIIH to complete the PIC formation and regulates enzymatic activities of TFIIH. However, the mode of binding between TFIIE and TFIIH is poorly understood. Here, we demonstrate the specific binding of the C‐terminal acidic domain (AC‐D) of the human TFIIEα subunit to the pleckstrin homology domain (PH‐D) of the human TFIIH p62 subunit and describe the solution structures of the free and PH‐D‐bound forms of AC‐D. Although the flexible N‐terminal acidic tail from AC‐D wraps around PH‐D, the core domain of AC‐D also interacts with PH‐D. AC‐D employs an entirely novel binding mode, which differs from the amphipathic helix method used by many transcriptional activators. So the binding surface between PH‐D and AC‐D is much broader than the specific binding surface between PH‐D and the p53 acidic fragments. From our in vitro studies, we demonstrate that this interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription.