The intracisternal A-particle upstream element interacts with transcription factor YY1 to activate transcription: Pleiotropic effects of YY1 on distinct DNA promoter elements

K. Satyamoorthy, K. Park, M. L. Atchison, C. C. Howe

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    Abstract

    Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65- kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, δ, or UCRBP), a zinc finger protein related to the Kruppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > κE3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.

    Original languageEnglish
    Pages (from-to)6621-6628
    Number of pages8
    JournalMolecular and Cellular Biology
    Volume13
    Issue number11
    Publication statusPublished - 1993

    Fingerprint

    Intracisternal A-Particle Genes
    YY1 Transcription Factor
    Methylation
    Carrier Proteins
    DNA
    Immunoglobulin kappa-Chains
    Moloney murine leukemia virus
    Embryonal Carcinoma Stem Cells
    Endoderm
    Nucleotide Motifs
    Terminal Repeat Sequences
    Zinc Fingers
    Protein Binding
    Transcription Factors
    Gels
    Proteins

    All Science Journal Classification (ASJC) codes

    • Molecular Biology
    • Cell Biology

    Cite this

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    abstract = "Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65- kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, δ, or UCRBP), a zinc finger protein related to the Kruppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > κE3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.",
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    AU - Park, K.

    AU - Atchison, M. L.

    AU - Howe, C. C.

    PY - 1993

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    N2 - Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65- kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, δ, or UCRBP), a zinc finger protein related to the Kruppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > κE3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.

    AB - Murine intracisternal A-particle long terminal repeats contain an intracisternal A-particle upstream enhancer (IUE) element that binds to a 65- kDa IUE binding protein (IUEB) present in both undifferentiated F9 embryonal carcinoma cells and differentiated parietal endoderm-like PYS-2 cells. This IUE element confers a CpG methylation-sensitive IUEB binding and enhancer activity. Using gel retardation, methylation interference, CpG methylation sensitivity binding, and cotransfection assays, we have now identified the 65-kDa IUEB as YY1 (also called NF-E1, δ, or UCRBP), a zinc finger protein related to the Kruppel family. YY1 binds to a number of similar but distinct DNA motifs, and cotransfection assays indicate that these motifs have different enhancer potentials in PYS-2 cells. The relative strengths of these elements are as follows: IUE > κE3' from the human immunoglobulin kappa light-chain 3' enhancer > upstream conserved region from the Moloney murine leukemia virus promoter. Results of DNA binding assays suggest that the differences in enhancer potentials are due to the different binding affinities of YY1 to the various motifs and the binding of two other transcription factors to the IUE sequence.

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