Characterization of Functional Domains within the Multifunctional Transcription Factor, YY1 (∗)

YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus a...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-12, Vol.270 (50), p.30213-30220
Main Authors: Bushmeyer, Sarah, Park, Kyoungsook, Atchison, Michael L.
Format: Article
Language:English
Subjects:
3T3 Cells
Animals
Base Sequence
Binding Sites
Blotting, Western
Cell Line
Chloramphenicol O-Acetyltransferase - analysis
Chloramphenicol O-Acetyltransferase - biosynthesis
Cloning, Molecular
DNA - metabolism
DNA Primers
DNA-Binding Proteins - chemistry
DNA-Binding Proteins - isolation & purification
DNA-Binding Proteins - metabolism
Electrophoresis, Polyacrylamide Gel
Erythroid-Specific DNA-Binding Factors
Mice
Molecular Sequence Data
Mutagenesis
Mutagenesis, Site-Directed
Nuclear Proteins - chemistry
Nuclear Proteins - metabolism
Polymerase Chain Reaction
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Restriction Mapping
Sequence Deletion
Spodoptera
Transcription Factors - chemistry
Transcription Factors - isolation & purification
Transcription Factors - metabolism
Transfection
YY1 Transcription Factor
Zinc Fingers
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Summary:YY1 is a multifunctional transcription factor capable of either activation or repression of transcription. Using a series of mutant proteins, we have characterized domains responsible for activation or repression. We found that the YY1 transcriptional activation domain lies near the amino terminus and requires amino acids 16-29 and 80-100 for maximal activity. The region between residues 16 and 29 has the potential to form an acidic amphipathic helix, whereas residues between 80 and 100 are rich in proline and glutamine. The YY1 repression domain lies near the carboxyl terminus and is embedded within the YY1 zinc finger region necessary for binding to DNA. Deletion of YY1 amino acids, which include zinc fingers 3 and 4, abolishes repression. However, site-directed mutagenesis, progressive deletion, and internal deletion mutant analyses indicate that the normal structures of zinc fingers 3 and 4 are not required for repression.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.50.30213