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Interaction of Hepatocyte nuclear factor 4alpha (HNF4alpha) with the TATA box binding protein (TBP) contributes to TFIID recruitment and HNF4alpha dependent transcription
Author(s) -
Takahashi Hidehisa,
MartinBrown Skylar,
Washburn Michael P.,
Florens Laurence,
Conaway Joan W.,
Conaway Ronald C.
Publication year - 2009
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.23.1_supplement.660.12
Subject(s) - transcription factor ii a , tata box binding protein , transcription factor ii d , hepatocyte nuclear factors , general transcription factor , taf2 , tata binding protein , tata box , promoter , transcription factor , transcription factor ii b , biology , microbiology and biotechnology , genetics , dna binding protein , enhancer , gene , gene expression
HNF4alpha, a member of nuclear hormone receptor superfamily, is a key transcriptional regulator of many genes that control glucose and lipid metabolism. We have identified HNF4alpha as an interaction partner of the general transcription factor TFIID and of its TATA‐box binding subunit TBP. HNF4alpha binds directly to TBP in vitro and in vivo through HNF4alpha residues 52‐174, which include the DNA binding and hinge domains. We have demonstrated that in vitro, HNF4alpha recruits TFIID or TBP to an immobilized template through direct physical interactions with TBP. An HNF4alpha point mutant that fails to interact with TBP does not recruit TBP or TFIID to promoters in vitro. The same mutation interferes with HNF4alpha‐dependent activation of a reporter gene in vivo. These observations, together with results indicating that HNF4alpha can activate transcription in a highly purified, reconstituted transcription system lacking coregulators, are consistent with the model that the interaction of HNF4alpha with TBP contributes to HNF4alpha‐induced transcription.