Dr1 is a general negative regulator of class II and class III gene expression. It binds to the basic repeat domain of TBP on promoter DNA and can prevent the RNA polymerase II holoenzyme, or its TFIIB and/or TFIIA subunits, from assembling into an initiation complex. Dr1 is phosphorylated in vivo and this modification affects its interaction with TBP. In addition, Dr1 interacts with the hyperphosphorylated form of Pol II and with the repression domain of the AREB6 repressor. Dr1 forms a heterodimer complex with DRAP1 through its histone fold domain. More recently it was discovered that Dr1-DRAP1 is a bi-functional basal transcription factor that differentially regulates gene transcription through DPE (downstream promoter elements) or TATA box motifs. It can stimulate transcription in vitro from Drosophila promoters containing DPEs, whereas it represses transcription from TATA-containing promoters.
Forme physique
Clear and colorless frozen liquid solution
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Use a manual defrost freezer and avoid repeated freeze-thaw cycles. While working, please keep sample on ice.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 1
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Not applicable
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Not applicable
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Science (New York, N.Y.), 266(5184), 448-450 (1994-10-21)
RNA polymerases I, II, and III each use the TATA-binding protein (TBP). Regulators that target this shared factor may therefore provide a means to coordinate the activities of the three nuclear RNA polymerases. The repressor Dr1 binds to TBP and
We have discovered a protein termed Dr1 that interacts with the TATA-binding protein, TBP. The association of Dr1 with TBP results in repression of both basal and activated levels of transcription. The interaction of Dr1 with TBP precludes the formation
A Dr1-associated polypeptide (DRAP1) was isolated from HeLa cells and found to function as a corepressor of transcription. Corepressor function requires an interaction between DRAP1 and Dr1. Heterodimer formation was dependent on a histone fold motif present at the amino
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