Open AccessFunctional Dissection of a Human Dr1-DRAP1 Repressor Complex
Author(s) -
Kam C. Yeung,
S Kim,
Danny Reinberg
Publication year - 1997
Publication title -
molecular and cellular biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.14
H-Index - 327
eISSN - 1067-8824
pISSN - 0270-7306
DOI - 10.1128/mcb.17.1.36
Subject(s) - corepressor , repressor , psychological repression , tata binding protein , biology , tata box binding protein , tata box , transcription (linguistics) , b3 domain , microbiology and biotechnology , gatad2b , transcription factor , promoter , genetics , dna binding protein , gene , gene expression , linguistics , philosophy
The heterotetrameric Dr1-DRAP1 transcriptional repressor complex was functionally dissected. Dr1 was found to contain two domains required for repression of transcription. The tethering domain interacts with the TATA box binding protein and directs the repressor complex to the promoter. This tethering domain can be replaced by a domain conferring sequence-specific recognition to the repressor complex. In the absence of the tethering domain, Dr1 interacts with its corepressor DRAP1, but this interaction is not functional. The enhancement of Dr1-mediated repression of transcription by DRAP1 requires the tethering domain. The second domain of Dr1 is the repression domain, which is glutamine-alanine rich. A 65-amino-acid polypeptide containing the repression domain fused to the Ga14 DNA binding domain repressed transcription when directed to TATA-containing and TATA-less promoters. This repression domain was also found to functionally and directly interact with the TATA box binding protein.