共查询到20条相似文献,搜索用时 15 毫秒
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Repression of promoter activity by CNOT2, a subunit of the transcription regulatory Ccr4-not complex 总被引:1,自引:0,他引:1
Zwartjes CG Jayne S van den Berg DL Timmers HT 《The Journal of biological chemistry》2004,279(12):10848-10854
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Implication of Ccr4-Not complex function in mRNA quality control in Saccharomyces cerevisiae 总被引:1,自引:0,他引:1
Assenholt J Mouaikel J Saguez C Rougemaille M Libri D Jensen TH 《RNA (New York, N.Y.)》2011,17(10):1788-1794
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Panasenko O Landrieux E Feuermann M Finka A Paquet N Collart MA 《The Journal of biological chemistry》2006,281(42):31389-31398
In this work, we determine that the Saccharomyces cerevisiae Ccr4-Not complex controls ubiquitination of the conserved ribosome-associated heterodimeric EGD (enhancer of Gal4p DNA binding) complex, which consists of the Egd1p and Egd2p subunits in yeast and is named NAC (nascent polypeptide-associated complex) in mammals. We show that the EGD complex subunits are ubiquitinated proteins, whose ubiquitination status is regulated during cell growth. Egd2p has a UBA domain that is not essential for interaction with Egd1p but is required for stability of Egd2p and Egd1p. Ubiquitination of Egd1p requires Not4p. Ubiquitination of Egd2p also requires Not4p, an intact Not4p RING finger domain, and all other subunits of the Ccr4-Not complex tested. In the absence of Not4p, Egd2p mislocalizes to punctuate structures. Finally, the EGD complex can be ubiquitinated in vitro by Not4p and Ubc4p, one of the E2 enzymes with which Not4p can interact. Taken together our results reveal that the EGD ribosome-associated complex is ubiquitinated in a regulated manner, and they show a new role for the Ccr4-Not complex in this ubiquitination. 相似文献
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The Ccr4-Not complex independently controls both Msn2-dependent transcriptional activation--via a newly identified Glc7/Bud14 type I protein phosphatase module--and TFIID promoter distribution
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Lenssen E James N Pedruzzi I Dubouloz F Cameroni E Bisig R Maillet L Werner M Roosen J Petrovic K Winderickx J Collart MA De Virgilio C 《Molecular and cellular biology》2005,25(1):488-498
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The Ccr4-Not complex is a conserved multi-subunit complex in eukaryotes that carries 2 enzymatic activities: ubiquitination mediated by the Not4 RING E3 ligase and deadenylation mediated by the Ccr4 and Caf1 orthologs. This complex has been implicated in all aspects of the mRNA life cycle, from synthesis of mRNAs in the nucleus to their degradation in the cytoplasm. More recently the complex has also been implicated in many aspects of the life cycle of proteins, from quality control during synthesis of peptides, to assembly of protein complexes and protein degradation. Consistently, the Ccr4-Not complex is found both in the nucleus, where it is connected to transcribing ORFs, and in the cytoplasm, where it was revealed to be both associated with translating ribosomes and in RNA processing bodies. This functional and physical presence of the Ccr4-Not complex at all stages of gene expression raises the question of its fundamental role. This review will summarize recent evidence designing the Not3/5 module of the Ccr4-Not complex as a functional module involved in coordination of the regulation of gene expression between the nucleus and the cytoplasm. 相似文献