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In vitro activity of the transcription activation functions of the progesterone receptor. Evidence for intermediary factors.
- Source :
-
The Journal of biological chemistry [J Biol Chem] 1992 Jan 25; Vol. 267 (3), pp. 1834-9. - Publication Year :
- 1992
-
Abstract
- The human progesterone receptor (hPR) is a ligand-dependent transcription factor which contains two distinct transcription activation functions (TAFs). The full-length hPR and its individual TAFs were overexpressed in the baculovirus system and tested in a HeLa cell-derived in vitro transcription system. hPR stimulated transcription in a ligand-independent manner. When the two TAFs fused to the DNA-binding domain of GAL4 were tested, only the constitutive TAF-1 was functional in vitro, strongly suggesting that the transcriptional activity of baculovirus-expressed hPR comes solely from TAF-1. The GAL-TAF-1 activator was found to self-squelch without affecting basal transcription. A partially purified fraction relieved this self-squelching and, moreover, stimulated transcriptional activation by GAL-TAF-1, while having no influence on basal transcription. These results strongly suggest that the transcriptional activity of GAL-TAF-1 requires a factor(s) distinct from the general transcription factors.
- Subjects :
- Animals
Baculoviridae
Base Sequence
Genetic Vectors
HeLa Cells
Humans
Insecta
Kinetics
Molecular Sequence Data
Oligodeoxyribonucleotides
Polymerase Chain Reaction
Receptors, Progesterone genetics
Receptors, Progesterone isolation & purification
Recombinant Fusion Proteins isolation & purification
Recombinant Fusion Proteins metabolism
Restriction Mapping
TATA Box
Templates, Genetic
Transcription Factors genetics
Transcription Factors isolation & purification
beta-Galactosidase genetics
beta-Galactosidase isolation & purification
beta-Galactosidase metabolism
Receptors, Progesterone metabolism
Transcription Factors metabolism
Transcription, Genetic
Subjects
Details
- Language :
- English
- ISSN :
- 0021-9258
- Volume :
- 267
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- The Journal of biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 1730721