PUBLICATION
A zebrafish ftz-f1 (Fushi tarazu factor 1) homologue requires multiple subdomains in the d and e regions for its transcriptional activity
- Authors
- Liu, D., Chandy, M., Lee, S.K., Le Drean, Y., Ando, H., Xiong, F., Lee, J.W., and Hew, C.L.
- ID
- ZDB-PUB-000505-25
- Date
- 2000
- Source
- The Journal of biological chemistry 275(22): 16758-16766 (Journal)
- Registered Authors
- Ando, Hideki
- Keywords
- none
- MeSH Terms
-
- Amino Acid Sequence
- Animals
- Base Sequence
- DNA Primers
- Dimerization
- Fushi Tarazu Transcription Factors
- Homeodomain Proteins/chemistry
- Homeodomain Proteins/genetics
- Homeodomain Proteins/metabolism*
- Molecular Sequence Data
- Mutagenesis
- Sequence Homology, Amino Acid
- Transcription, Genetic*
- Transcriptional Activation
- Zebrafish
- PubMed
- 10747875 Full text @ J. Biol. Chem.
Citation
Liu, D., Chandy, M., Lee, S.K., Le Drean, Y., Ando, H., Xiong, F., Lee, J.W., and Hew, C.L. (2000) A zebrafish ftz-f1 (Fushi tarazu factor 1) homologue requires multiple subdomains in the d and e regions for its transcriptional activity. The Journal of biological chemistry. 275(22):16758-16766.
Abstract
A zebrafish Ftz-F1 homologue, zFF1A (zebrafish Ff1a or Nr5a2, a member of nuclear receptor superfamily) and its C-terminally truncated variant (zFF1B) were previously identified. Due to lack of the identity box (I-box) and activation function 2 domain (AF-2), zFF1B lacks transactivation function and fails to synergize with ligand-bound estrogen receptor (ER) in regulating target promoters. It was speculated that the I-box might be involved in the zFF1A/ER interaction. In the present study, the function of the I-box was examined. In the absence of the I-box or with an altered heptad 9 in the I-box, the AF-2 of zFF1A was not functional, either in the presence or absence of ER. The GST pull down assay showed that zFF1A, as well as its mutants exerted similar physical contacts with ER-LBD, suggesting that the 'dimerization' domain (I-box) is in fact essential for the transcriptional activity of zFF1A. Moreover, the nuclear receptor coactivator selectively activated zFF1 with the I-box, but exerted no effect on zFF1B, indicating that the I-box, as well as the AF-2, are able to interact with the coactivators. By deletion study and analysis of the identified domains in GAL4-DBD, other regions of zFF1A critical for its activation function (AF) were also delineated. Consistent with the mutation analysis, AF-2 was active only in the presence of the I-box. We also identified a novel AF domain (AF-3) located in the hinge region (aa 155-267), although the activity of AF-3 was inhibited by its flanking region. We suggest that the D and E regions of zFF1A possess both positive and negative transactivation functions, and inter-domain "cross-talk" may confer the full transcriptional activity of the protein.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping