PUBLICATION
The DBP transcriptional activation domain is highly homologous to that of HLF and TEF and is not responsible for the tissue type-specific transcriptional activity of DBP
- Authors
- Li, S. and Hunger, S.P.
- ID
- ZDB-PUB-010308-2
- Date
- 2001
- Source
- Gene 263(1-2): 239-245 (Journal)
- Registered Authors
- Keywords
- Basic leucine zipper proteins, Proline and acidic amino acid rich proteins, Transcription factor
- MeSH Terms
-
- 3T3 Cells
- Amino Acid Sequence
- Animals
- Basic-Leucine Zipper Transcription Factors
- Binding Sites/genetics
- Chloramphenicol O-Acetyltransferase/genetics
- Chloramphenicol O-Acetyltransferase/metabolism
- DNA, Recombinant
- DNA-Binding Proteins/chemistry
- DNA-Binding Proteins/genetics*
- Humans
- Mice
- Molecular Sequence Data
- Plasmids/genetics
- Protein Binding
- Protein Structure, Tertiary
- Recombinant Fusion Proteins/genetics
- Recombinant Fusion Proteins/metabolism
- Sequence Deletion
- Sequence Homology, Amino Acid
- Transcription Factors/genetics*
- Transcriptional Activation
- Tumor Cells, Cultured
- Zebrafish Proteins*
- PubMed
- 11223263 Full text @ Gene
Citation
Li, S. and Hunger, S.P. (2001) The DBP transcriptional activation domain is highly homologous to that of HLF and TEF and is not responsible for the tissue type-specific transcriptional activity of DBP. Gene. 263(1-2):239-245.
Abstract
DBP, HLF and TEF comprise a distinct subfamily of mammalian bZIP proteins that plays an important role in regulation of tissue-specific gene expression, particularly in the liver. In this report we demonstrate that DBP contains a 38 amino acid TAD which is highly homologous to the HLF and TEF TADs that we have delineated previously. Deletion of this domain completely abrogates transcriptional activity of native DBP and GAL4-DBP fusion proteins. This domain functions as a modular TAD that is a potent transcriptional activator when fused to the GAL4 DBD. While DBP itself is a liver-specific transactivator, the DBP TAD is active in a variety of cell types, indicating that liver-specific activity is not an intrinsic property of the TAD and must be conferred by other regions of the protein. Using GAL4-HLF fusion proteins, we further refine the core TAD of PAR proteins to a region of 13 amino acids. Recently described PAR-bZIP proteins from Drosophila and zebrafish also contain domains that share strong homology with the TAD of mammalian PAR proteins, making this one of the most highly evolutionarily conserved TADs identified to date.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping