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Competitive recruitment of CBP and Rb-HDAC regulates UBF acetylation and ribosomal transcription.
- Source :
-
Molecular cell [Mol Cell] 2000 Nov; Vol. 6 (5), pp. 1059-66. - Publication Year :
- 2000
-
Abstract
- RNA polymerase I (PolI) transcription is activated by the HMG box architectural factor UBF, which loops approximately 140 bp of DNA into the enhancesome, necessitating major chromatin remodeling. Here we show that the acetyltransferase CBP is recruited to and acetylates UBF both in vitro and in vivo. CBP activates PolI transcription in vivo through its acetyltransferase domain and acetylation of UBF facilitates transcription derepression and activation in vitro. CBP activation and Rb suppression of ribosomal transcription by recruitment to UBF are mutually exclusive, regulating in vivo PolI transcription through an acetylation-deacetylation "flip-flop." Thus, PolI transcription is regulated by protein acetylation, and the competitive recruitment of CBP and Rb.
- Subjects :
- 3T3 Cells
Acetylation
Animals
Binding, Competitive
CREB-Binding Protein
Chromatin chemistry
Chromatin genetics
Chromatin metabolism
DNA Footprinting
DNA-Binding Proteins chemistry
Enzyme Activation
Histone Deacetylases chemistry
Mice
Models, Genetic
Nuclear Proteins antagonists & inhibitors
Nuclear Proteins chemistry
Promoter Regions, Genetic genetics
Protein Binding
Protein Structure, Tertiary
RNA Polymerase I metabolism
Rats
Retinoblastoma Protein antagonists & inhibitors
Substrate Specificity
Trans-Activators antagonists & inhibitors
Trans-Activators chemistry
Transcription Factors chemistry
Xenopus laevis genetics
DNA-Binding Proteins metabolism
Histone Deacetylases metabolism
Nuclear Proteins metabolism
Pol1 Transcription Initiation Complex Proteins
Retinoblastoma Protein metabolism
Ribosomes genetics
Trans-Activators metabolism
Transcription Factors metabolism
Transcription, Genetic
Subjects
Details
- Language :
- English
- ISSN :
- 1097-2765
- Volume :
- 6
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Molecular cell
- Publication Type :
- Academic Journal
- Accession number :
- 11106745
- Full Text :
- https://doi.org/10.1016/s1097-2765(00)00104-0