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      RP58 associates with condensed chromatin and mediates a sequence-specific transcriptional repression.

      The Journal of Biological Chemistry
      Amino Acid Sequence, Animals, Base Sequence, Binding Sites, COS Cells, Chromatin, metabolism, Cloning, Molecular, Consensus Sequence, DNA, Humans, Microscopy, Electron, Molecular Sequence Data, Repressor Proteins, genetics, Transcription Factors, Transcription, Genetic

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          Abstract

          An approximately 120-amino acid domain present generally at the NH2 termini, termed the POZ domain, is highly conserved in various proteins with zinc finger DNA binding motifs. We have isolated a novel protein sharing homology with the POZ domain of a number of zinc finger proteins, including the human BCL-6 protein. By using a binding site selection technique (CAST), a high affinity binding site of the protein was determined to be (A/C)ACATCTG(G/T)(A/C), containing the E box core sequence motif. The protein was shown to repress transcription from a promoter linked to its target sequences and was hence named RP58 (Repressor Protein with a predicted molecular mass of 58 kDa). Immunogold electron microscopic study revealed that almost all RP58 is localized in condensed chromatin regions. These observations demonstrate for the first time that a protein mediating a sequence-specific transcriptional repression associates with highly condensed chromatin. We suggest that RP58 may be involved in a molecular link between sequence-specific transcriptional repression and the organization of chromosomes in the nucleus.

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