Albert, TK

Boelens, R

Collart, MA

de Ruwe, MJ

Hanzawa, H

Legtenberg, YIA

Timmers, HTM

van den Heuvel, FAJ

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.</p

Dissertations of the University of Groningen

Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex

Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex

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Dissertations of the University of Groningen