Open AccessStructural analysis and dimerization potential of the human TAF5 subunit of TFIID
Author(s) -
S. Bhattacharya,
Shinako Takada,
Raymond H. Jacobson
Publication year - 2007
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.0610297104
Subject(s) - taf1 , transcription factor ii d , transcription factor ii a , taf4 , taf2 , biology , general transcription factor , microbiology and biotechnology , protein subunit , rna polymerase ii , genetics , transcription preinitiation complex , computational biology , transcription factor , rna polymerase , rna , gene , promoter , gene expression , enhancer
TFIID is an essential factor required for RNA polymerase II transcription but remains poorly understood because of its intrinsic complexity. Human TAF5, a 100-kDa subunit of general transcription factor TFIID, is an essential gene and plays a critical role in assembling the 1.2 MDa TFIID complex. We report here a structural analysis of the TAF5 protein. Our structure at 2.2-Å resolution of the TAF5-NTD2 domain reveals an α-helical domain with distant structural similarity to RNA polymerase II CTD interacting factors. The TAF5-NTD2 domain contains several conserved clefts likely to be critical for TFIID complex assembly. Our biochemical analysis of the human TAF5 protein demonstrates the ability of the N-terminal half of the TAF5 gene to form a flexible, extended dimer, a key property required for the assembly of the TFIID complex.