Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID

K F Stringer; C J Ingles; J Greenblatt

doi:10.1038/345783a0

Direct and selective binding of an acidic transcriptional activation domain to the TATA-box factor TFIID

Nature. 1990 Jun 28;345(6278):783-6. doi: 10.1038/345783a0.

Authors

K F Stringer¹, C J Ingles, J Greenblatt

Affiliation

¹ Banting and Best Department of Medical Research, University of Toronto, Ontario, Canada.

PMID: 2193231
DOI: 10.1038/345783a0

Abstract

The potent transactivation domain of the herpes simplex virion protein VP16 was used as a column ligand for affinity chromatography. VP16 binds strongly and highly selectively to the human and yeast TATA box-binding factors. Our results imply that the principal target for acidic activation domains is the TATA-box factor TFIID.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Chromatography, Affinity
HeLa Cells
Herpes Simplex
Humans
Phosphoproteins / metabolism*
Phosphoproteins / ultrastructure
Protein Binding
RNA Polymerase II / metabolism
Regulatory Sequences, Nucleic Acid*
Saccharomyces cerevisiae / genetics
Trans-Activators / metabolism*
Trans-Activators / ultrastructure
Transcription Factors / metabolism*
Transcription Factors / ultrastructure

Substances

Phosphoproteins
Trans-Activators
Transcription Factors
RNA Polymerase II