Abstract
The KRAB repression domain is one of the most widely distributed transcriptional effector domains yet identified, but its mechanism of repression is unknown. We have cloned a corepressor, KAP-1, which associates with the KRAB domain but not with KRAB mutants that have lost repression activity. KAP-1 can enhance KRAB-mediated repression and is a repressor when directly tethered to DNA. KAP-1 contains a RING finger, B boxes, and a PHD finger; the RING-B1-B2 structure is required for KRAB binding and corepression. We propose that KAP-1 may be a universal corepressor for the large family of KRAB domain-containing transcription factors.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Cattle
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Cloning, Molecular
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Consensus Sequence
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics*
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Deoxyribonucleoproteins / chemistry
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Gene Expression Regulation
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Macromolecular Substances
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Nuclear Proteins / metabolism
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PAX3 Transcription Factor
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Paired Box Transcription Factors
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Protein Binding
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Repressor Proteins / chemistry
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Repressor Proteins / genetics*
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Sequence Alignment
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Sequence Homology, Amino Acid
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Transcription Factors*
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Tripartite Motif-Containing Protein 28
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Zinc Fingers*
Substances
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DNA-Binding Proteins
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Deoxyribonucleoproteins
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Macromolecular Substances
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Nuclear Proteins
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PAX3 Transcription Factor
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PAX3 protein, human
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Paired Box Transcription Factors
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Repressor Proteins
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Transcription Factors
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Pax3 protein, mouse
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Trim28 protein, mouse
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Tripartite Motif-Containing Protein 28