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Transcriptional regulation of the Drosophila catalase gene by the DRE/DREF system.
- Source :
-
Nucleic acids research [Nucleic Acids Res] 2004 Feb 24; Vol. 32 (4), pp. 1318-24. Date of Electronic Publication: 2004 Feb 24 (Print Publication: 2004). - Publication Year :
- 2004
-
Abstract
- Reactive oxygen species (ROS) cause oxidative stress and aging. The catalase gene is a key component of the cellular antioxidant defense network. However, the molecular mechanisms that regulate catalase gene expression are poorly understood. In this study, we have identified a DNA replication-related element (DRE; 5'-TATCGATA) in the 5'-flanking region of the Drosophila catalase gene. Gel mobility shift assays revealed that a previously identified factor called DREF (DRE- binding factor) binds to the DRE sequence in the Drosophila catalase gene. We used site-directed mutagenesis and in vitro transient transfection assays to establish that expression of the catalase gene is regulated by DREF through the DRE site. To explore the role of DRE/DREF in vivo, we established transgenic flies carrying a catalase-lacZ fusion gene with or without mutation in the DRE. The beta-galactosidase expression patterns of these reporter transgenic lines demonstrated that the catalase gene is upregulated by DREF through the DRE sequence. In addition, we observed suppression of the ectopic DREF-induced rough eye phenotype by a catalase amorphic Cat(n1) allele, indicating that DREF activity is modulated by the intracellular redox state. These results indicate that the DRE/DREF system is a key regulator of catalase gene expression and provide evidence of cross-talk between the DRE/DREF system and the antioxidant defense system.
- Subjects :
- 5' Flanking Region
Animals
Binding Sites
Drosophila anatomy & histology
Drosophila enzymology
Eye anatomy & histology
Gene Expression Regulation, Enzymologic
Genes, Insect
Mutation
Phenotype
Catalase genetics
Drosophila genetics
Drosophila Proteins
Response Elements
Transcription Factors physiology
Transcriptional Activation
Subjects
Details
- Language :
- English
- ISSN :
- 1362-4962
- Volume :
- 32
- Issue :
- 4
- Database :
- MEDLINE
- Journal :
- Nucleic acids research
- Publication Type :
- Academic Journal
- Accession number :
- 14982956
- Full Text :
- https://doi.org/10.1093/nar/gkh302