Transcriptional repression by a novel member of the bZIP family of transcription factors.
We describe here a novel member of the bZIP family of DNA-binding proteins, designated E4BP4, that displays an unusual DNA-binding specificity which overlaps that of the activating transcription factor family of factors. When expressed in a transient transfection assay with a suitable reporter plasmid, E4BP4 strongly repressed transcription in a DNA-binding-site-dependent manner. Examination of a series of deletion mutants revealed that sequences responsible for the repressing potential of E4BP4 lie within the carboxyl-terminal region of the protein. No similarity was found between this region and the repressing domains of other known eukaryotic transcriptional repressors.
Cowell
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Gene Transcription Laboratory, Imperial Cancer Research Fund, Hammersmith Hospital, London, England.
Skinner
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Hurst
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D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D050976:Basic-Leucine Zipper Transcription Factors; D001665:Binding Sites; D004252:DNA Mutational Analysis; D004268:DNA-Binding Proteins / Q000235:genetics*; D051790:G-Box Binding Factors; D008969:Molecular Sequence Data; D005810:Multigene Family / Q000235:genetics; D010920:Placenta; D010940:Plant Proteins / Q000235:genetics*; D011487:Protein Conformation; D012097:Repressor Proteins / Q000235:genetics*; D012689:Sequence Homology, Nucleic Acid; D014157:Transcription Factors; D014158:Transcription, Genetic; D014162:Transfection
D050976:Basic-Leucine Zipper Transcription Factors; D004268:DNA-Binding Proteins; D051790:G-Box Binding Factors; C497440:NFIL3 protein, human; D010940:Plant Proteins; D012097:Repressor Proteins; D014157:Transcription Factors