Abstract
A DNA-binding site selection and enrichment procedure revealed a sequence-specific DNA-binding activity selectively associated with glutathione S-transferase-retinoblastoma protein chimeras (GST-RB) that had been incubated with a human cell extract. Appropriate mutant forms of GST-RB, incubated in equivalent extracts, did not associate with this specific DNA-binding activity, and a peptide replica of the HPV E7 RB-binding segment selectively inhibited the association of GST-RB with the sequence-specific DNA-binding protein(s). Sequence analysis of oligonucleotides with high affinity for GST-RB complexes, as well as the results of competition binding studies, strongly suggest that RB can associate specifically with the transcription factor E2F or with a protein having closely related DNA-binding properties.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Adenovirus Early Proteins
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Base Sequence
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Binding Sites
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Carrier Proteins*
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Cell Cycle Proteins*
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DNA-Binding Proteins / metabolism*
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E2F Transcription Factors
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Glutathione Transferase / genetics
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Macromolecular Substances
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Molecular Sequence Data
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Oligodeoxyribonucleotides / metabolism
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Oncogene Proteins, Viral / metabolism*
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Protein Binding
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Recombinant Fusion Proteins
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Regulatory Sequences, Nucleic Acid
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Retinoblastoma Protein / metabolism*
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Retinoblastoma-Binding Protein 1
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Transcription Factor DP1
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Transcription Factors / metabolism*
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Transcription, Genetic
Substances
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Adenovirus Early Proteins
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Carrier Proteins
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Cell Cycle Proteins
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DNA-Binding Proteins
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E2F Transcription Factors
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Macromolecular Substances
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Oligodeoxyribonucleotides
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Oncogene Proteins, Viral
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Recombinant Fusion Proteins
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Retinoblastoma Protein
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Retinoblastoma-Binding Protein 1
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Transcription Factor DP1
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Transcription Factors
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Glutathione Transferase