Transcriptional activation through ETS domain binding sites in the cytochrome c oxidase subunit IV gene
- Northwestern Univ., Chicago, IL (United States)
A mutational analysis of the rat cytochrome c oxidase subunit IV (RCO4) promoter region revealed the presence of a major control element consisting of a tandemly repeated pair of binding sites for a nuclear factor from HeLa cells. This factor was designated NRF-2 (nuclear respiratory factor 2) because a functional recognition site was also found in the human ATP synthase {beta}-subunit gene. Deletion or site-directed point mutations of the NRF-2 binding sites in the RCO4 promoter resulted in substantial loss of transcriptional activity, and synthetic oligomers of the NRF-2 binding sites from both genes stimulated a heterologous promoter when cloned in cis. NRF-2 binding a transcriptional activation required a purine-rich core sequence, GGAA. This motif is characteristic of the recognition site for a family of activators referred to as ETS domain proteins because of the similarity within their DNA-binding domains to the ets-1 proto-oncogene product. NRF-2 recognized an authentic Ets-1 site within the Moloney murine sarcoma virus long terminal repeat, and this site was able to compete for NRF-2 binding to the RCO4 promoter sequence. However, in contrast to Ets-1, which appears to be exclusive to lymphoid tissues, NRF-2 has the broad tissue distribution expected of a regulator of respiratory chain expression.
- OSTI ID:
- 5089817
- Journal Information:
- Molecular and Cellular Biology; (United States), Vol. 11:11; ISSN 0270-7306
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
CYTOCHROME OXIDASE
GENE REGULATION
GENE REPRESSORS
DNA SEQUENCING
TRANSCRIPTION
MOLECULAR BIOLOGY
GENE MUTATIONS
HELA CELLS
OLIGONUCLEOTIDES
ONCOGENIC VIRUSES
RATS
ANIMALS
ENZYMES
HAEM DEHYDROGENASES
MAMMALS
MICROORGANISMS
MUTATIONS
NUCLEIC ACIDS
ORGANIC COMPOUNDS
OXIDOREDUCTASES
PARASITES
PROTEINS
RODENTS
STRUCTURAL CHEMICAL ANALYSIS
VERTEBRATES
VIRUSES
550200* - Biochemistry