Article
- The EMBO Journal (1999) 18, 6662 - 6671
- doi:10.1093/emboj/18.23.6662
A new regulatory domain on the TATA-binding protein
Yong Cang1, David T. Auble2 and Gregory Prelich1
- Department of Molecular Genetics, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA
- Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908, USA
Correspondence to:
Gregory Prelich, E-mail: prelich@aecom.yu.edu
Received 5 August 1999; Accepted 7 October 1999; Revised 7 October 1999
Abstract
Recognition of the TATA box by the TATA-binding protein (TBP) is a highly regulated step in RNA polymerase II-dependent transcription. Several proteins have been proposed to regulate TBP activity, yet the TBP domains responsive to all these regulators have not been defined. Here we describe a new class of TBP mutants that increase transcription from core promoters in vivo. The majority of these mutations alter amino acids that cluster tightly on the TBP surface, defining a new TBP regulatory domain. The mutant TBP proteins are defective for binding the transcriptional regulator yNC2, are resistant to inhibition by yNC2 in vitro and exhibit allele-specific genetic interactions with yNC2. These results provide strong biochemical and genetic evidence that TBP is directly repressed in vivo, and define a new TBP domain important for transcriptional regulation.
Keywords:
- BUR6,
- NC2,
- repression,
- TBP,
- transcription
