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

Albert, Thomas K
Hanzawa, Hiroyuki
Legtenberg, Yvonne I A
de Ruwe, Marjolein J
van den Heuvel, Fiona A J
Boelens, Rolf
Timmers, H Th Marc
Published in EMBO journal. 2002, vol. 21, no. 3, p. 355-64
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.
Keywords Amino Acid SequenceDNA-Binding Proteins/geneticsFungal Proteins/geneticsLigases/geneticsModels, MolecularMolecular Sequence DataRepressor Proteins/geneticsRibonucleasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTranscription Factors/geneticsTranscription, GeneticUbiquitin-Conjugating EnzymesUbiquitin-Protein Ligases
PMID: 11823428
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Research group Caractérisation génétique et biochimique du complexe Ccr4-Not conservé (81)
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ALBERT, Thomas K et al. Identification of a ubiquitin-protein ligase subunit within the CCR4-NOT transcription repressor complex. In: EMBO journal, 2002, vol. 21, n° 3, p. 355-64. doi: 10.1093/emboj/21.3.355 https://archive-ouverte.unige.ch/unige:30066

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Deposited on : 2013-10-01

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