Open AccessIdentification of human TFIID components and direct interaction between a 250-kDa polypeptide and the TATA box-binding protein (TFIID tau).
Author(s) -
Ritsuko Takada,
Yoshihiro Nakatani,
Alexander Hoffmann,
Tetsuro Kokubo,
S. Hasegawa,
Robert G. Roeder,
Masami Horikoshi
Publication year - 1992
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.89.24.11809
Subject(s) - taf1 , transcription factor ii a , taf4 , transcription factor ii d , tata box , taf2 , tata box binding protein , biology , microbiology and biotechnology , transcription factor , genetics , dna binding protein , promoter , gene , gene expression , enhancer
Previous studies have indicated that human transcription initiation factor TFIID is a large complex that contains a TATA-binding polypeptide (TFIID tau or TBP) and other components that qualitatively alter promoter interactions and are uniquely required for activator-dependent (versus basal) transcription. TFIID tau-specific antibody columns have been employed to identify a number of human TFIID polypeptides that are tightly associated with TFIID tau. These differ in size from polypeptides in known general initiation factors, including the initiator-binding factor (TFII-I) which shares some promoter binding characteristics with TFIID. The largest component (p250) identified in TFIID was shown to interact directly and tightly with TFIID tau, suggesting that it may play a major role in the assembly of the TFIID complex.