Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex.
The RING finger protein CNOT4 is a component of the CCR4-NOT complex. This complex is implicated in repression of RNA polymerase II transcription. Here we demonstrate that CNOT4 functions as a ubiquitin-protein ligase (E3). We show that the unique C4C4 RING domain of CNOT4 interacts with a subset of ubiquitin-conjugating ... enzymes (E2s). Using NMR spectroscopy, we detail the interaction of CNOT4 with UbcH5B and characterize RING residues that are critical for this interaction. CNOT4 acts as a potent E3 ligase in vitro. Mutations that destabilize the E2-E3 interface abolish this activity. Based on these results, we present a model of how E3 ligase function within the CCR4-NOT complex relates to transcriptional regulation.
Mesh Terms:
Amino Acid Sequence, DNA-Binding Proteins, Fungal Proteins, Ligases, Models, Molecular, Molecular Sequence Data, Repressor Proteins, Ribonucleases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
Amino Acid Sequence, DNA-Binding Proteins, Fungal Proteins, Ligases, Models, Molecular, Molecular Sequence Data, Repressor Proteins, Ribonucleases, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription Factors, Transcription, Genetic, Ubiquitin-Conjugating Enzymes, Ubiquitin-Protein Ligases
EMBO J.
Date: Feb. 01, 2002
PubMed ID: 11823428
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