Dr1, a TATA-binding protein-associated phosphoprotein and inhibitor of class II gene transcription
A Inostroza, FH Mermelstein, I Ha, WS Lane… - Cell, 1992 - cell.com
A Inostroza, FH Mermelstein, I Ha, WS Lane, D Reinberg
Cell, 1992•cell.comWe havediscovered a protein termed Drl that interacts with the TATA-binding protein, TBP.
The association of Drl with TBP results in repression of both basal and activated levels of
transcription. The interaction of Drl with TBP precludes the formation of a
transcriptioncompetent complex by inhibiting the association of TFIIA and/or TFIIB with TBP.
Drl activity is associated with a 19 kd protein. A cDNA clone encoding Drl was isolated. Drl is
phosphorylated In vivo and phosphorylation of Drl affected its interaction with TBP. Our …
The association of Drl with TBP results in repression of both basal and activated levels of
transcription. The interaction of Drl with TBP precludes the formation of a
transcriptioncompetent complex by inhibiting the association of TFIIA and/or TFIIB with TBP.
Drl activity is associated with a 19 kd protein. A cDNA clone encoding Drl was isolated. Drl is
phosphorylated In vivo and phosphorylation of Drl affected its interaction with TBP. Our …
Summary
We havediscovered a protein termed Drl that interacts with the TATA-binding protein, TBP. The association of Drl with TBP results in repression of both basal and activated levels of transcription. The interaction of Drl with TBP precludes the formation of a transcriptioncompetent complex by inhibiting the association of TFIIA and/or TFIIB with TBP. Drl activity is associated with a 19 kd protein. A cDNA clone encoding Drl was isolated. Drl is phosphorylated In vivo and phosphorylation of Drl affected its interaction with TBP. Our results suggest a regulatory role for Drl in repression of transcription mediated via phosphorylation.
cell.com