A DNA-binding protein containing two widely separated zinc finger motifs that recognize the same DNA sequence
Autor: | Tom Maniatis, Chen-Ming Fan |
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Rok vydání: | 1990 |
Předmět: |
Protein Conformation
Molecular Sequence Data Restriction Mapping Regulatory Sequences Nucleic Acid Biology Methylation Cell Line chemistry.chemical_compound Recognition sequence Sequence Homology Nucleic Acid Complementary DNA Metalloproteins Genetics Humans Amino Acid Sequence Cloning Molecular Promoter Regions Genetic Zinc finger Base Sequence Binding protein Protein primary structure Promoter DNA Molecular biology Zinc finger nuclease DNA-Binding Proteins Zinc Gene Expression Regulation chemistry Interferon Type I Transcription Factors Developmental Biology |
Zdroj: | Genes & Development. 4:29-42 |
ISSN: | 1549-5477 0890-9369 |
Popis: | 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. |
Databáze: | OpenAIRE |
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