Abstract
The activator of stromelysin 1 gene transcription, SPBP, interacts with the RING finger protein RNF4. Both proteins are ubiquitously expressed and localized in the nucleus. RNF4 facilitates accumulation of specific SPBP-DNA complexes in vitro and acts as a positive cofactor in SPBP-mediated transactivation. SPBP harbors an internal zinc finger of the PHD/LAP type. This domain can form intra-chain protein-protein contacts in SPBP resulting in negative modulation of SPBP-RNF4 interaction.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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Cell Nucleus / metabolism
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DNA-Binding Proteins / metabolism
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Escherichia coli
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Fibroblasts / metabolism
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Humans
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Matrix Metalloproteinase 3 / genetics
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Mice
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Molecular Sequence Data
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Nuclear Proteins*
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Peptide Mapping
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Protein Binding
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Saccharomyces cerevisiae
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Transcription Factors / metabolism*
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Transcription, Genetic
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Transcriptional Activation
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Ubiquitin-Protein Ligases
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Zinc Fingers*
Substances
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DNA-Binding Proteins
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Nuclear Proteins
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RNF4 protein, human
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TCF20 protein, human
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Transcription Factors
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Rnf4 protein, mouse
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Ubiquitin-Protein Ligases
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Matrix Metalloproteinase 3