The mammalian TFIID protein is present in two functionally distinct complexes.
Open Access
- 1 November 1991
- journal article
- Published by Cold Spring Harbor Laboratory in Genes & Development
- Vol. 5 (11), 1946-1956
- https://doi.org/10.1101/gad.5.11.1946
Abstract
The TFIID activity recognizes a TATA-box element and supports formation of an initiation complex containing RNA polymerase II. Antisera specific for the 38-kD human TFIID protein were used to determine whether this protein cofractionated with the TFIID activity. Surprisingly, the TFIID activity in HeLa whole-cell extracts was resolved into two different size complexes, one of 300 kD and one of greater than 700 kD. Cofractionation studies suggest that both complexes contain the 38-kD protein; thus, this component of the large complexes is probably responsible for recognition of the TATA sequence and interaction with the other general transcription factors in formation of the initiation complex. Interestingly, in contrast to the TFIID activity characterized previously, the 300-kD form of TFIID activity, B-TFIID, does not support stimulation of transcription by factors containing acidic or glutamine-rich activating motifs. We propose that the functional and physical differences between these two forms of TFIID activity are caused by differences in the protein composition of the TFIID complexes of which the 38-kD hTFIID protein is an integral part.Keywords
This publication has 36 references indexed in Scilit:
- Three-dimensional structure of yeast RNA polymerase II at 16 Å resolutionCell, 1991
- Mechanism of action of an acidic transcriptional activator in vitroCell, 1991
- Activation domains of stably bound GAL4 derivatives alleviate repression of promoters by nucleosomesCell, 1991
- Mechanism of transcriptional activation by Sp1: Evidence for coactivatorsCell, 1990
- Cloning and structure of a yeast gene encoding a general transcription initiation factor TFIID that binds to the TATA boxNature, 1989
- Function of a yeast TATA element-binding protein in a mammalian transcription systemNature, 1988
- A yeast activity can substitute for the HeLa cell TATA box factorNature, 1988
- Transcription Elements and Factors of Rna Polymerase B Promoters of Higher EukaryoteCritical Reviews in Biochemistry, 1988
- Interaction of a gene-specific transcription factor with the adenovirus major late promoter upstream of the TATA box regionCell, 1985
- Formation of stable preinitiation complexes between eukaryotic class B transcription factors and promoter sequencesNature, 1983