| Literature DB >> 11823428 |
Thomas K Albert1, Hiroyuki Hanzawa, Yvonne I A Legtenberg, Marjolein J de Ruwe, Fiona A J van den Heuvel, Martine A Collart, Rolf Boelens, H Th Marc Timmers.
Abstract
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.Entities:
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Year: 2002 PMID: 11823428 PMCID: PMC125831 DOI: 10.1093/emboj/21.3.355
Source DB: PubMed Journal: EMBO J ISSN: 0261-4189 Impact factor: 11.598