Identification of a ubiquitin–protein ligase subunit within the CCR4–NOT transcription repressor complex
AUTOR(ES)
Albert, Thomas K.
FONTE
Oxford University Press
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=125831Documentos Relacionados
- Functional Domains of the Rsp5 Ubiquitin-Protein Ligase
- The ubiquitin–protein ligase Itch regulates p73 stability
- The large subunit of RNA polymerase II is a substrate of the Rsp5 ubiquitin-protein ligase
- Localization of the Rsp5p Ubiquitin-Protein Ligase at Multiple Sites within the Endocytic Pathway
- The E6–AP Ubiquitin–Protein Ligase (UBE3A) Gene Is Localized within a Narrowed Angelman Syndrome Critical Region
