A DNA-binding protein containing two widely separated zinc finger motifs that recognize the same DNA sequence.
We have isolated a full-length cDNA clone encoding a protein (PRDII-BF1) that binds specifically to a positive regulatory domain (PRDII) of the human IFN-beta gene promoter, and to a similar sequence present in a number of other promoters and enhancers. The sequence of this protein reveals two novel structural features. ... First, it is the largest sequence-specific DNA-binding protein reported to date (298 kD). Second, it contains two widely separated sets of C2-H2-type zinc fingers. Remarkably, each set of zinc fingers binds to the same DNA sequence motif with similar affinities and methylation interference patterns. Thus, this protein may act by binding simultaneously to reiterated copies of the same recognition sequence. Although the function of PRDII-BF1 is not known, the level of its mRNA is inducible by serum and virus, albeit with different kinetics.
Mesh Terms:
Amino Acid Sequence, Base Sequence, Cell Line, Cloning, Molecular, DNA, DNA-Binding Proteins, Gene Expression Regulation, Humans, Interferon Type I, Metalloproteins, Methylation, Molecular Sequence Data, Promoter Regions, Genetic, Protein Conformation, Regulatory Sequences, Nucleic Acid, Restriction Mapping, Sequence Homology, Nucleic Acid, Transcription Factors, Zinc
Amino Acid Sequence, Base Sequence, Cell Line, Cloning, Molecular, DNA, DNA-Binding Proteins, Gene Expression Regulation, Humans, Interferon Type I, Metalloproteins, Methylation, Molecular Sequence Data, Promoter Regions, Genetic, Protein Conformation, Regulatory Sequences, Nucleic Acid, Restriction Mapping, Sequence Homology, Nucleic Acid, Transcription Factors, Zinc
Genes Dev.
Date: Jan. 01, 1990
PubMed ID: 2106471
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