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

Lenssen, Eve; James, Nicole; Pedruzzi, Ivo; Dubouloz, F; Cameroni, Elisabetta; Bisig, R.; Maillet, Laurent; Werner, Michel; Roosen, Johnny; Petrović, Katarina; Winderickx, Joris; Collart, Martine A.; Virgilio, Claudio De

doi:10.1128/mcb.25.1.488-498.2005

Cited by 65 publications

(69 citation statements)

References 58 publications

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“…This treatment is thought to produce aberrantly folded proteins in vivo. Interestingly, deletion of NOT4 also gives rise to resistance to heat shock, which is most likely to result from derepression of HSP gene expression under noninducing conditions (Lenssen et al 2005). We found that the role of the RING finger of Not4p in tolerance to acute heat shock is independent of HSP gene expression (Figure 6).…”

Section: Discussionmentioning

confidence: 69%

“…This suggests that the ubiquitin protein ligase activity of Not4p, together with Ubc4p and/or Ubc5p, is involved in regulation of this stress response. Tolerance to acute heat stress in ubc4Dubc5D, not5D, and not4D strains has been linked with increased levels of heat-shock gene expression under normal growth conditions (Seufert and Jentsch 1990;Lenssen et al 2002Lenssen et al , 2005. Therefore, Northern blot analysis was performed to determine the level of heat-shock gene expression in the RING-finger mutant strains.…”

Section: Resultsmentioning

confidence: 99%

“…Moreover, deletion of genes encoding Ccr4-Not subunits resulted in derepression of several stressresponse element (STRE)-regulated genes in an Msn2p-Msn4p-dependent manner (Lenssen et al 2002). This function is controlled by the Glc7p-Bud14p phosphatase (Lenssen et al 2005) and is responsible for expression of HSP genes following heat shock (Martinez-Pastor et al 1996).…”

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confidence: 99%

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Modulation of Ubc4p/Ubc5p-Mediated Stress Responses by the RING-Finger-Dependent Ubiquitin-Protein Ligase Not4p in Saccharomyces cerevisiae

Mulder

Inagaki

Cameroni³

et al. 2007

Genetics

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The Ccr4-Not complex consists of nine subunits and acts as a regulator of mRNA biogenesis in Saccharomyces cerevisiae. The human ortholog of yeast NOT4, CNOT4, displays UbcH5B-dependent ubiquitinprotein ligase (E3 ligase) activity in a reconstituted in vitro system. However, an in vivo role for this enzymatic activity has not been identified. Site-directed mutagenesis of the RING finger of yeast Not4p identified residues required for interaction with Ubc4p and Ubc5p, the yeast orthologs of UbcH5B. Subsequent in vitro assays with purified Ccr4-Not complexes showed Not4p-mediated E3 ligase activity, which was dependent on the interaction with Ubc4p. To investigate the in vivo relevance of this activity, we performed synthetic genetic array (SGA) analyses using not4D and not4L35A alleles. This indicates involvement of the RING finger of Not4p in transcription, ubiquitylation, and DNA damage responses. In addition, we found a phenotypic overlap between deletions of UBC4 and mutants encoding single-aminoacid substitutions of the RING finger of Not4p. Together, our results show that Not4p functions as an E3 ligase by modulating Ubc4p/Ubc5p-mediated stress responses in vivo.

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Section: Discussionmentioning

confidence: 69%

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 99%

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Modulation of Ubc4p/Ubc5p-Mediated Stress Responses by the RING-Finger-Dependent Ubiquitin-Protein Ligase Not4p in Saccharomyces cerevisiae

Mulder

Inagaki

Cameroni³

et al. 2007

Genetics

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“…A second mechanism for PKA-mediated regulation of STRE-controlled gene expression involves the Ccr4-Not complex, a global transcriptional regulator that affects genes positively and negatively. It was proposed that this complex contributes to the downregulation of Msn2/4-driven transcription and this through direct interaction with Tpk2 and by modulation of the phosphorylation status of Msn2 via the Bud14-Glc7 protein phosphatase (Lenssen et al 2002(Lenssen et al , 2005. Moreover, PKA seems to additionally inhibit the function of Msn2 and Msn4 via the protein kinases Yak1 and Rim15.…”

Section: Regulation Of the Camp-pka Pathwaymentioning

confidence: 99%

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

et al. 2010

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Cells of all living organisms contain complex signal transduction networks to ensure that a wide range of physiological properties are properly adapted to the environmental conditions. The fundamental concepts and individual building blocks of these signalling networks are generally well-conserved from yeast to man; yet, the central role that growth factors and hormones play in the regulation of signalling cascades in higher eukaryotes is executed by nutrients in yeast. Several nutrient-controlled pathways, which regulate cell growth and proliferation, metabolism and stress resistance, have been defined in yeast. These pathways are integrated into a signalling network, which ensures that yeast cells enter a quiescent, resting phase (G 0 ) to survive periods of nutrient scarceness and that they rapidly resume growth and cell proliferation when nutrient conditions become favourable again. A series of well-conserved nutrient-sensory protein kinases perform key roles in this signalling network: i.e. Snf1, PKA, Tor1 and Tor2, Sch9 and Pho85-Pho80. In this review, we provide a comprehensive overview on the current understanding of the signalling processes mediated via these kinases with a particular focus on how these individual pathways converge to signalling networks that ultimately ensure the dynamic translation of extracellular nutrient signals into appropriate physiological responses.

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“…Additionally, not4 mutations suppress the transcriptional defect caused by Ty insertions into the HIS4 promoter (Badarinarayana et al 2000), a phenotype also seen in spt15 (TBP), spt3, and mot1 mutants (Jiang and Stillman 1996;Madison and Winston 1997;Winston and Sudarsanam 1998). Mutations in genes encoding the Ccr4-Not complex affect binding of TBP and TAF1 to promoters (Lenssen et al 2005).…”

Section: Genetic Interactions Of Nhp6 and Gcn5 With Mot1mentioning

confidence: 99%

Genetic Interactions Between Nhp6 and Gcn5 With Mot1 and the Ccr4–Not Complex That Regulate Binding of TATA-Binding Protein in Saccharomyces cerevisiae

Biswas

Mitra

et al. 2006

Genetics

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Our previous work suggests that the Nhp6 HMGB protein stimulates RNA polymerase II transcription via the TATA-binding protein TBP and that Nhp6 functions in the same functional pathway as the Gcn5 histone acetyltransferase. In this report we examine the genetic relationship between Nhp6 and Gcn5 with the Mot1 and Ccr4-Not complexes, both of which have been implicated in regulating DNA binding by TBP. We find that combining either a nhp6ab or a gcn5 mutation with mot1, ccr4, not4, or not5 mutations results in lethality. Combining spt15 point mutations (in TBP) with either mot1 or ccr4 also results in either a growth defect or lethality. Several of these synthetic lethalities can be suppressed by overexpression of TFIIA, TBP, or Nhp6, suggesting that these genes facilitate formation of the TBP-TFIIA-DNA complex. The growth defect of a not5 mutant can be suppressed by a mot1 mutant. HO gene expression is reduced by nhp6ab, gcn5, or mot1 mutations, and the additive decreases in HO mRNA levels in nhp6ab mot1 and gcn5 mot1 strains suggest different modes of action. Chromatin immunoprecipitation experiments show decreased binding of TBP to promoters in mot1 mutants and a further decrease when combined with either nhp6ab or gcn5 mutations.

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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

Cited by 65 publications

References 58 publications

Modulation of Ubc4p/Ubc5p-Mediated Stress Responses by the RING-Finger-Dependent Ubiquitin-Protein Ligase Not4p in Saccharomyces cerevisiae

Modulation of Ubc4p/Ubc5p-Mediated Stress Responses by the RING-Finger-Dependent Ubiquitin-Protein Ligase Not4p in Saccharomyces cerevisiae

Life in the midst of scarcity: adaptations to nutrient availability in Saccharomyces cerevisiae

Genetic Interactions Between Nhp6 and Gcn5 With Mot1 and the Ccr4–Not Complex That Regulate Binding of TATA-Binding Protein in Saccharomyces cerevisiae

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