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Journal articles on the topic 'Saccharomyces cerevisiae, cell cycle, Snf1'

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Published: 9 March 2023

Last updated: 31 July 2025

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1

Soontorngun, Nitnipa, Marc Larochelle, Simon Drouin, François Robert, and Bernard Turcotte. "Regulation of Gluconeogenesis in Saccharomyces cerevisiae Is Mediated by Activator and Repressor Functions of Rds2." Molecular and Cellular Biology 27, no. 22 (2007): 7895–905. http://dx.doi.org/10.1128/mcb.01055-07.

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ABSTRACT In Saccharomyces cerevisiae, RDS2 encodes a zinc cluster transcription factor with unknown function. Here, we unravel a key function of Rds2 in gluconeogenesis using chromatin immunoprecipitation-chip technology. While we observed that Rds2 binds to only a few promoters in glucose-containing medium, it binds many additional genes when the medium is shifted to ethanol, a nonfermentable carbon source. Interestingly, many of these genes are involved in gluconeogenesis, the tricarboxylic acid cycle, and the glyoxylate cycle. Importantly, we show that Rds2 has a dual function: it directly

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Newcomb, Laura L., Jasper A. Diderich, Matthew G. Slattery, and Warren Heideman. "Glucose Regulation of Saccharomyces cerevisiae Cell Cycle Genes." Eukaryotic Cell 2, no. 1 (2003): 143–49. http://dx.doi.org/10.1128/ec.2.1.143-149.2003.

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ABSTRACT Nutrient-limited Saccharomyces cerevisiae cells rapidly resume proliferative growth when transferred into glucose medium. This is preceded by a rapid increase in CLN3, BCK2, and CDC28 mRNAs encoding cell cycle regulatory proteins that promote progress through Start. We have tested the ability of mutations in known glucose signaling pathways to block glucose induction of CLN3, BCK2, and CDC28. We find that loss of the Snf3 and Rgt2 glucose sensors does not block glucose induction, nor does deletion of HXK2, encoding the hexokinase isoenzyme involved in glucose repression signaling. Rap

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Timblin, Barbara K., Kelly Tatchell, and Lawrence W. Bergman. "Deletion of the Gene Encoding the Cyclin-Dependent Protein Kinase Pho85 Alters Glycogen Metabolism in Saccharomyces cerevisiae." Genetics 143, no. 1 (1996): 57–66. http://dx.doi.org/10.1093/genetics/143.1.57.

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Abstract Pho85, a protein kinase with significant homology to the cyclin-dependent kinase, Cdc28, has been shown to function in repression of transcription of acid phosphatase (APase, encoded by PHO5) in high phosphate (Pi) medium, as well as in regulation of the cell cycle at G1/S. We describe several unique phenotypes associated with the deletion of the PHO85 gene including growth defects on a variety of carbon sources and hyperaccumulation of glycogen in rich medium high in Pi. Hyperaccumulation of glycogen in the pho85 strains is independent of other APase regulatory molecules and is not s

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Gray, Joseph V., Gregory A. Petsko, Gerald C. Johnston, Dagmar Ringe, Richard A. Singer, and Margaret Werner-Washburne. "“Sleeping Beauty”: Quiescence in Saccharomyces cerevisiae." Microbiology and Molecular Biology Reviews 68, no. 2 (2004): 187–206. http://dx.doi.org/10.1128/mmbr.68.2.187-206.2004.

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SUMMARY The cells of organisms as diverse as bacteria and humans can enter stable, nonproliferating quiescent states. Quiescent cells of eukaryotic and prokaryotic microorganisms can survive for long periods without nutrients. This alternative state of cells is still poorly understood, yet much benefit is to be gained by understanding it both scientifically and with reference to human health. Here, we review our knowledge of one “model” quiescent cell population, in cultures of yeast grown to stationary phase in rich media. We outline the importance of understanding quiescence, summarize the p

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Miura, Natsuko, Masahiro Shinohara, Yohei Tatsukami, et al. "Spatial Reorganization of Saccharomyces cerevisiae Enolase To Alter Carbon Metabolism under Hypoxia." Eukaryotic Cell 12, no. 8 (2013): 1106–19. http://dx.doi.org/10.1128/ec.00093-13.

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ABSTRACTHypoxia has critical effects on the physiology of organisms. In the yeastSaccharomyces cerevisiae, glycolytic enzymes, including enolase (Eno2p), formed cellular foci under hypoxia. Here, we investigated the regulation and biological functions of these foci. Focus formation by Eno2p was inhibited temperature independently by the addition of cycloheximide or rapamycin or by the single substitution of alanine for the Val22 residue. Using mitochondrial inhibitors and an antioxidant, mitochondrial reactive oxygen species (ROS) production was shown to participate in focus formation. Focus f

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Dombek, Kenneth M., Valentina Voronkova, Alexa Raney, and Elton T. Young. "Functional Analysis of the Yeast Glc7-Binding Protein Reg1 Identifies a Protein Phosphatase Type 1-Binding Motif as Essential for Repression of ADH2 Expression." Molecular and Cellular Biology 19, no. 9 (1999): 6029–40. http://dx.doi.org/10.1128/mcb.19.9.6029.

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ABSTRACT In Saccharomyces cerevisiae, the protein phosphatase type 1 (PP1)-binding protein Reg1 is required to maintain complete repression of ADH2 expression during growth on glucose. Surprisingly, however, mutant forms of the yeast PP1 homologue Glc7, which are unable to repress expression of another glucose-regulated gene, SUC2, fully repressed ADH2. ConstitutiveADH2 expression in reg1 mutant cells did require Snf1 protein kinase activity like constitutive SUC2expression and was inhibited by unregulated cyclic AMP-dependent protein kinase activity like ADH2 expression in derepressed cells.

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7

Huang, Dongqing, Jason Moffat, Wayne A. Wilson, et al. "Cyclin Partners Determine Pho85 Protein Kinase Substrate Specificity In Vitro and In Vivo: Control of Glycogen Biosynthesis by Pcl8 and Pcl10." Molecular and Cellular Biology 18, no. 6 (1998): 3289–99. http://dx.doi.org/10.1128/mcb.18.6.3289.

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ABSTRACT In Saccharomyces cerevisiae, PHO85 encodes a cyclin-dependent protein kinase (Cdk) with multiple roles in cell cycle and metabolic controls. In association with the cyclin Pho80, Pho85 controls acid phosphatase gene expression through phosphorylation of the transcription factor Pho4. Pho85 has also been implicated as a kinase that phosphorylates and negatively regulates glycogen synthase (Gsy2), and deletion of PHO85 causes glycogen overaccumulation. We report that the Pcl8/Pcl10 subgroup of cyclins directs Pho85 to phosphorylate glycogen synthase both in vivo and in vitro. Disruption

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8

Miller, M. E., B. R. Cairns, R. S. Levinson, K. R. Yamamoto, D. A. Engel, and M. M. Smith. "Adenovirus E1A specifically blocks SWI/SNF-dependent transcriptional activation." Molecular and Cellular Biology 16, no. 10 (1996): 5737–43. http://dx.doi.org/10.1128/mcb.16.10.5737.

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Expression of the adenovirus E1A243 oncoprotein in Saccharomyces cerevisiae produces a slow-growth phenotype with accumulation of cells in the G1 phase of the cell cycle. This effect is due to the N-terminal and CR1 domains of E1A243, which in rodent cells are involved in triggering cellular transformation and also in binding to the cellular transcriptional coactivator p300. A genetic screen was undertaken to identify genes required for the function of E1A243 in S. cerevisiae. This screen identified SNF12, a gene encoding the 73-kDa subunit of the SWI/SNF transcriptional regulatory complex. Mu

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9

Neef, Daniel W., and Michael P. Kladde. "Polyphosphate Loss Promotes SNF/SWI- and Gcn5-Dependent Mitotic Induction of PHO5." Molecular and Cellular Biology 23, no. 11 (2003): 3788–97. http://dx.doi.org/10.1128/mcb.23.11.3788-3797.2003.

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ABSTRACT Approximately 800 transcripts in Saccharomyces cerevisiae are cell cycle regulated. The oscillation of ∼40% of these genes, including a prominent subclass involved in nutrient acquisition, is not understood. To address this problem, we focus on the mitosis-specific activation of the phosphate-responsive promoter, PHO5. We show that the unexpected mitotic induction of the PHO5 acid phosphatase in rich medium requires the transcriptional activators Pho4 and Pho2, the cyclin-dependent kinase inhibitor Pho81, and the chromatin-associated enzymes Gcn5 and Snf2/Swi2. PHO5 mitotic activation

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10

Barber, Louise J., Thomas A. Ward, John A. Hartley, and Peter J. McHugh. "DNA Interstrand Cross-Link Repair in the Saccharomyces cerevisiae Cell Cycle: Overlapping Roles for PSO2 (SNM1) with MutS Factors and EXO1 during S Phase." Molecular and Cellular Biology 25, no. 6 (2005): 2297–309. http://dx.doi.org/10.1128/mcb.25.6.2297-2309.2005.

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ABSTRACT Pso2/Snm1 is a member of the β-CASP metallo-β-lactamase family of proteins that include the V(D)J recombination factor Artemis. Saccharomyces cerevisiae pso2 mutants are specifically sensitive to agents that induce DNA interstrand cross-links (ICLs). Here we establish a novel overlapping function for PSO2 with MutS mismatch repair factors and the 5′-3′ exonuclease Exo1 in the repair of DNA ICLs, which is confined to S phase. Our data demonstrate a requirement for NER and Pso2, or Exo1 and MutS factors, in the processing of ICLs, and this is required prior to the repair of ICL-induced

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11

Treitel, Michelle A., Sergei Kuchin, and Marian Carlson. "Snf1 Protein Kinase Regulates Phosphorylation of the Mig1 Repressor in Saccharomyces cerevisiae." Molecular and Cellular Biology 18, no. 11 (1998): 6273–80. http://dx.doi.org/10.1128/mcb.18.11.6273.

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ABSTRACT In glucose-grown cells, the Mig1 DNA-binding protein recruits the Ssn6-Tup1 corepressor to glucose-repressed promoters in the yeastSaccharomyces cerevisiae. Previous work showed that Mig1 is differentially phosphorylated in response to glucose. Here we examine the role of Mig1 in regulating repression and the role of the Snf1 protein kinase in regulating Mig1 function. Immunoblot analysis of Mig1 protein from a snf1 mutant showed that Snf1 is required for the phosphorylation of Mig1; moreover, hxk2 andreg1 mutations, which relieve glucose inhibition of Snf1, correspondingly affect pho

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12

Honigberg, Saul M., and Rita H. Lee. "Snf1 Kinase Connects Nutritional Pathways Controlling Meiosis in Saccharomyces cerevisiae." Molecular and Cellular Biology 18, no. 8 (1998): 4548–55. http://dx.doi.org/10.1128/mcb.18.8.4548.

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ABSTRACT Glucose inhibits meiosis in Saccharomyces cerevisiae at three different steps (IME1 transcription, IME2transcription, and entry into late stages of meiosis). Because many of the regulatory effects of glucose in yeast are mediated through the inhibition of Snf1 kinase, a component of the glucose repression pathway, we determined the role of SNF1 in regulating meiosis. Deleting SNF1 repressed meiosis at the same three steps that were inhibited by glucose, suggesting that glucose blocks meiosis by inhibiting Snf1. For example, the snf1Δ mutant completely failed to induce IME1 transcripts

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13

Elbing, Karin, Rhonda R. McCartney, and Martin C. Schmidt. "Purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae." Biochemical Journal 393, no. 3 (2006): 797–805. http://dx.doi.org/10.1042/bj20051213.

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Members of the Snf1/AMPK family of protein kinases are activated by distinct upstream kinases that phosphorylate a conserved threonine residue in the Snf1/AMPK activation loop. Recently, the identities of the Snf1- and AMPK-activating kinases have been determined. Here we describe the purification and characterization of the three Snf1-activating kinases of Saccharomyces cerevisiae. The identities of proteins associated with the Snf1-activating kinases were determined by peptide mass fingerprinting. These kinases, Sak1, Tos3 and Elm2 do not appear to require the presence of additional subunits

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Hubbard, E. J., R. Jiang, and M. Carlson. "Dosage-dependent modulation of glucose repression by MSN3 (STD1) in Saccharomyces cerevisiae." Molecular and Cellular Biology 14, no. 3 (1994): 1972–78. http://dx.doi.org/10.1128/mcb.14.3.1972-1978.1994.

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The SNF1 protein kinase of Saccharomyces cerevisiae is required to relieve glucose repression of transcription. To identify components of the SNF1 pathway, we isolated multicopy suppressors of defects caused by loss of SNF4, an activator of the SNF1 kinase. Increased dosage of the MSN3 gene restored invertase expression in snf4 mutants and also relieved glucose repression in the wild type. Deletion of MSN3 caused no substantial phenotype, and we identified a homolog, MTH1, encoding a protein 61% identical to MSN3. Both are also homologous to chicken fimbrin, human plastin, and yeast SAC6 over

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Kuchin, S., V. K. Vyas, and M. Carlson. "Role of the yeast Snf1 protein kinase in invasive growth." Biochemical Society Transactions 31, no. 1 (2003): 175–77. http://dx.doi.org/10.1042/bst0310175.

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The sucrose non-fermenting 1 (Snf1) protein kinase of Saccharomyces cerevisiae is important for transcriptional, metabolic and developmental responses to glucose limitation. Here we discuss the role of the Snf1 kinase in regulating filamentous invasive growth. Haploid invasive growth occurs in response to glucose limitation and requires FLO11, a gene encoding a cell-surface adhesin. Snf1 regulates transcription of FLO11 by antagonizing the function of two repressors, Nrg1 and Nrg2. Snf1 and the Nrg repressors also affect diploid pseudohyphal differentiation, which is a response to nitrogen lim

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Ye, Tian, Raúl García-Salcedo, José Ramos, and Stefan Hohmann. "Gis4, a New Component of the Ion Homeostasis System in the Yeast Saccharomyces cerevisiae." Eukaryotic Cell 5, no. 10 (2006): 1611–21. http://dx.doi.org/10.1128/ec.00215-06.

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ABSTRACT Gis4 is a new component of the system required for acquisition of salt tolerance in Saccharomyces cerevisiae. The gis4Δ mutant is sensitive to Na+ and Li+ ions but not to osmotic stress. Genetic evidence suggests that Gis4 mediates its function in salt tolerance, at least partly, together with the Snf1 protein kinase and in parallel with the calcineurin protein phosphatase. When exposed to salt stress, mutants lacking gis4Δ display a defect in maintaining low intracellular levels of Na+ and Li+ ions and exporting those ions from the cell. This defect is due to diminished expression of

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Hubbard, E. J., R. Jiang, and M. Carlson. "Dosage-dependent modulation of glucose repression by MSN3 (STD1) in Saccharomyces cerevisiae." Molecular and Cellular Biology 14, no. 3 (1994): 1972–78. http://dx.doi.org/10.1128/mcb.14.3.1972.

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The SNF1 protein kinase of Saccharomyces cerevisiae is required to relieve glucose repression of transcription. To identify components of the SNF1 pathway, we isolated multicopy suppressors of defects caused by loss of SNF4, an activator of the SNF1 kinase. Increased dosage of the MSN3 gene restored invertase expression in snf4 mutants and also relieved glucose repression in the wild type. Deletion of MSN3 caused no substantial phenotype, and we identified a homolog, MTH1, encoding a protein 61% identical to MSN3. Both are also homologous to chicken fimbrin, human plastin, and yeast SAC6 over

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Vyas, Valmik K., Sergei Kuchin, Cristin D. Berkey та Marian Carlson. "Snf1 Kinases with Different β-Subunit Isoforms Play Distinct Roles in Regulating Haploid Invasive Growth". Molecular and Cellular Biology 23, № 4 (2003): 1341–48. http://dx.doi.org/10.1128/mcb.23.4.1341-1348.2003.

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ABSTRACT The Snf1 protein kinase of Saccharomyces cerevisiae has been shown to have a role in regulating haploid invasive growth in response to glucose depletion. Cells contain three forms of the Snf1 kinase, each with a different β-subunit isoform, either Gal83, Sip1, or Sip2. We present evidence that different Snf1 kinases play distinct roles in two aspects of invasive growth, namely, adherence to the agar substrate and filamentation. The Snf1-Gal83 form of the kinase is required for adherence, whereas either Snf1-Gal83 or Snf1-Sip2 is sufficient for filamentation. Genetic evidence indicates

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Vyas, Valmik K., Sergei Kuchin, and Marian Carlson. "Interaction of the Repressors Nrg1 and Nrg2 With the Snf1 Protein Kinase in Saccharomyces cerevisiae." Genetics 158, no. 2 (2001): 563–72. http://dx.doi.org/10.1093/genetics/158.2.563.

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Abstract The Snf1 protein kinase is essential for the transcription of glucose-repressed genes in Saccharomyces cerevisiae. We identified Nrg2 as a protein that interacts with Snf1 in the two-hybrid system. Nrg2 is a C2H2 zinc-finger protein that is homologous to Nrg1, a repressor of the glucose- and Snf1-regulated STA1 (glucoamylase) gene. Snf1 also interacts with Nrg1 in the two-hybrid system and co-immunoprecipitates with both Nrg1 and Nrg2 from cell extracts. A LexA fusion to Nrg2 represses transcription from a promoter containing LexA binding sites, indicating that Nrg2 also functions as

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Celenza, J. L., and M. Carlson. "Mutational analysis of the Saccharomyces cerevisiae SNF1 protein kinase and evidence for functional interaction with the SNF4 protein." Molecular and Cellular Biology 9, no. 11 (1989): 5034–44. http://dx.doi.org/10.1128/mcb.9.11.5034-5044.1989.

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The SNF1 gene of Saccharomyces cerevisiae encodes a protein-serine/threonine kinase that is required for derepression of gene expression in response to glucose limitation. We present evidence that the protein kinase activity is essential for SNF1 function: substitution of Arg for Lys in the putative ATP-binding site results in a mutant phenotype. A polyhistidine tract near the N terminus was found to be dispensable. Deletion of the large region C terminal to the kinase domain only partially impaired SNF1 function, causing expression of invertase to be somewhat reduced but still glucose repress

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Sanz, Pascual, Katja Ludin, and Marian Carlson. "Sip5 Interacts With Both the Reg1/Glc7 Protein Phosphatase and the Snf1 Protein Kinase of Saccharomyces cerevisiae." Genetics 154, no. 1 (2000): 99–107. http://dx.doi.org/10.1093/genetics/154.1.99.

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Abstract The Snf1 protein kinase is an essential component of the glucose starvation signalling pathway in Saccharomyces cerevisiae. We have used the two-hybrid system to identify a new protein, Sip5, that interacts with the Snf1 kinase complex in response to glucose limitation. Coimmunoprecipitation studies confirmed the association of Sip5 and Snf1 in cell extracts. We found that Sip5 also interacts strongly with Reg1, the regulatory subunit of the Reg1/Glc7 protein phosphatase 1 complex, in both two-hybrid and coimmunoprecipitation assays. Previous work showed that Reg1/Glc7 interacts with

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Casamayor, Antonio, Raquel Serrano, María Platara, Carlos Casado, Amparo Ruiz, and Joaquín Ariño. "The role of the Snf1 kinase in the adaptive response of Saccharomyces cerevisiae to alkaline pH stress." Biochemical Journal 444, no. 1 (2012): 39–49. http://dx.doi.org/10.1042/bj20112099.

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Alkaline pH stress invokes a potent and fast transcriptional response in Saccharomyces cerevisiae that includes many genes repressed by glucose. Certain mutants in the glucose-sensing and -response pathways, such as those lacking the Snf1 kinase, are sensitive to alkalinization. In the present study we show that the addition of glucose to the medium improves the growth of wild-type cells at high pH, fully abolishes the snf1 alkali-sensitive phenotype and attenuates high pH-induced Snf1 phosphorylation at Thr210. Lack of Elm1, one of the three upstream Snf1 kinases (Tos3, Elm1 and Sak1), marked

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Wright, R. M., and R. O. Poyton. "Release of two Saccharomyces cerevisiae cytochrome genes, COX6 and CYC1, from glucose repression requires the SNF1 and SSN6 gene products." Molecular and Cellular Biology 10, no. 3 (1990): 1297–300. http://dx.doi.org/10.1128/mcb.10.3.1297-1300.1990.

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We show here that SNF1 and SSN6 are required for derepression of the glucose-repressible yeast genes COX6 and CYC1, which encode the mitochondrial proteins cytochrome c oxidase subunit VI and iso-1-cytochrome c, respectively. In an snf1 mutant genetic background, the transcription of both COX6 and CYC1 continued to be repressed after cells were shifted into derepressing media. In an ssn6 mutant genetic background, both COX6 and CYC1 were expressed constitutively at high levels in repressing media. SSN6 acted epistatically to SNF1 in the regulation of both cytochrome genes. These findings are s

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Kuchin, Sergei, Valmik K. Vyas, and Marian Carlson. "Snf1 Protein Kinase and the Repressors Nrg1 and Nrg2 Regulate FLO11, Haploid Invasive Growth, and Diploid Pseudohyphal Differentiation." Molecular and Cellular Biology 22, no. 12 (2002): 3994–4000. http://dx.doi.org/10.1128/mcb.22.12.3994-4000.2002.

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ABSTRACT The Snf1 protein kinase of Saccharomyces cerevisiae is important for many cellular responses to glucose limitation, including haploid invasive growth. We show here that Snf1 regulates transcription of FLO11, which encodes a cell surface glycoprotein required for invasive growth. We further show that Nrg1 and Nrg2, two repressor proteins that interact with Snf1, function as negative regulators of invasive growth and as repressors of FLO11. We also examined the role of Snf1, Nrg1, and Nrg2 in two other Flo11-dependent processes. Mutations affected the initiation of biofilm formation, wh

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Hedbacker, Kristina, Robert Townley, and Marian Carlson. "Cyclic AMP-Dependent Protein Kinase Regulates the Subcellular Localization of Snf1-Sip1 Protein Kinase." Molecular and Cellular Biology 24, no. 5 (2004): 1836–43. http://dx.doi.org/10.1128/mcb.24.5.1836-1843.2004.

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ABSTRACT The Snf1/AMP-activated protein kinase family has diverse roles in cellular responses to metabolic stress. In Saccharomyces cerevisiae, Snf1 protein kinase has three isoforms of the β subunit that confer versatility on the kinase and that exhibit distinct patterns of subcellular localization. The Sip1 β subunit resides in the cytosol in glucose-grown cells and relocalizes to the vacuolar membrane in response to carbon stress. We show that translation of Sip1 initiates at the second ATG of the open reading frame, yielding a potential site for N myristoylation, and that mutation of the c

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Hedbacker, Kristina, Seung-Pyo Hong, and Marian Carlson. "Pak1 Protein Kinase Regulates Activation and Nuclear Localization of Snf1-Gal83 Protein Kinase." Molecular and Cellular Biology 24, no. 18 (2004): 8255–63. http://dx.doi.org/10.1128/mcb.24.18.8255-8263.2004.

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ABSTRACT Three kinases, Pak1, Tos3, and Elm1, activate Snf1 protein kinase in Saccharomyces cerevisiae. This cascade is conserved in mammals, where LKB1 activates AMP-activated protein kinase. We address the specificity of the activating kinases for the three forms of Snf1 protein kinase containing the β-subunit isoforms Gal83, Sip1, and Sip2. Pak1 is the most important kinase for activating Snf1-Gal83 in response to glucose limitation, but Elm1 also has a significant role; moreover, both Pak1 and Elm1 affect Snf1-Sip2. These findings exclude the possibility of a one-to-one correspondence betw

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Muranaka, T., H. Banno, and Y. Machida. "Characterization of tobacco protein kinase NPK5, a homolog of Saccharomyces cerevisiae SNF1 that constitutively activates expression of the glucose-repressible SUC2 gene for a secreted invertase of S. cerevisiae." Molecular and Cellular Biology 14, no. 5 (1994): 2958–65. http://dx.doi.org/10.1128/mcb.14.5.2958-2965.1994.

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We have isolated a cDNA (cNPK5) that encodes a protein kinase of 511 amino acids from suspension cultures of tobacco cells. The predicted kinase domain of NPK5 is 65% identical in terms of amino acid sequence to that of the SNF1 serine/threonine protein kinase of Saccharomyces cerevisiae, which plays a central role in catabolite repression in yeast cells. SNF1 positively regulates transcription of various glucose-repressible genes of the yeast, such as the SUC2 gene for a secreted invertase, in response to glucose deprivation: snf1 mutants cannot utilize sucrose as a carbon source. Expression

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Hong, Seung-Pyo, Milica Momcilovic та Marian Carlson. "Function of Mammalian LKB1 and Ca2+/Calmodulin-dependent Protein Kinase Kinase α as Snf1-activating Kinases in Yeast". Journal of Biological Chemistry 280, № 23 (2005): 21804–9. http://dx.doi.org/10.1074/jbc.m501887200.

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The Snf1/AMP-activated protein kinase (AMPK) family is important for metabolic regulation in response to stress. In the yeast Saccharomyces cerevisiae, the Snf1 kinase cascade comprises three Snf1-activating kinases, Pak1, Tos3, and Elm1. The only established mammalian AMPK kinase is LKB1. We show that LKB1 functions heterologously in yeast. In pak1Δ tos3Δ elm1Δ cells, LKB1 activated Snf1 catalytic activity and conferred a Snf+ growth phenotype. Coexpression of STRADα and MO25α, which form a complex with LKB1, enhanced LKB1 function. Thus, the Snf1/AMPK kinase cascade is functionally conserved

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Ahuatzi, Deifilia, Alberto Riera, Rafael Peláez, Pilar Herrero, and Fernando Moreno. "Hxk2 Regulates the Phosphorylation State of Mig1 and Therefore Its Nucleocytoplasmic Distribution." Journal of Biological Chemistry 282, no. 7 (2006): 4485–93. http://dx.doi.org/10.1074/jbc.m606854200.

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Mig1 and Hxk2 are two major mediators of glucose repression in Saccharomyces cerevisiae. However, the mechanism by which Hxk2 participates in the glucose repression signaling pathway is not completely understood. Recently, it has been demonstrated that Hxk2 interacts with Mig1 to generate a repressor complex located in the nucleus of S. cerevisiae. However, the mechanism by which Mig1 favors the presence of Hxk2 in the nucleus is not clear, and the function of Hxk2 at the nuclear repressor complex level is still unknown. Here, we report that serine 311 of Mig1 is a critical residue for interac

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Thompson-Jaeger, S., J. François, J. P. Gaughran, and K. Tatchell. "Deletion of SNF1 affects the nutrient response of yeast and resembles mutations which activate the adenylate cyclase pathway." Genetics 129, no. 3 (1991): 697–706. http://dx.doi.org/10.1093/genetics/129.3.697.

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Abstract We have isolated a snf1/ccr1 mutant of Saccharomyces cerevisiae which loses viability upon starvation and fails to accumulate glycogen in response to abrupt depletion of phosphate or glucose. A snf1 null mutant is sensitive to heat stress and starvation and fails to accumulate glycogen during growth in rich medium. The phenotypes of the snf1 mutants are those commonly associated with an overactivation of the adenylate cyclase pathway. Mutations in adenylate cyclase or RAS2 which decrease the level of cAMP in the cell moderate the snf1 phenotype. In contrast, a mutation in RAS2 (RAS2va

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Shirra, Margaret K., Jana Patton-Vogt, Andreas Ulrich, et al. "Inhibition of Acetyl Coenzyme A Carboxylase Activity Restores Expression of the INO1 Gene in a snf1Mutant Strain of Saccharomyces cerevisiae." Molecular and Cellular Biology 21, no. 17 (2001): 5710–22. http://dx.doi.org/10.1128/mcb.21.17.5710-5722.2001.

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ABSTRACT Mutations in the Saccharomyces cerevisiae SNF1 gene affect a number of cellular processes, including the expression of genes involved in carbon source utilization and phospholipid biosynthesis. To identify targets of the Snf1 kinase that modulate expression of INO1, a gene required for an early, rate-limiting step in phospholipid biosynthesis, we performed a genetic selection for suppressors of the inositol auxotrophy ofsnf1Δ strains. We identified mutations inACC1 and FAS1, two genes important for fatty acid biosynthesis in yeast; ACC1 encodes acetyl coenzyme A carboxylase (Acc1), an

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Celenza, J. L., F. J. Eng, and M. Carlson. "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase." Molecular and Cellular Biology 9, no. 11 (1989): 5045–54. http://dx.doi.org/10.1128/mcb.9.11.5045-5054.1989.

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The SNF4 gene is required for expression of glucose-repressible genes in response to glucose deprivation in Saccharomyces cerevisiae. Previous evidence suggested that SNF4 is functionally related to SNF1, another essential gene in this global regulatory system that encodes a protein kinase. Increased SNF1 gene dosage partially compensates for a mutation in SNF4, and the SNF4 function is required for maximal SNF1 protein kinase activity in vitro. We have cloned SNF4 and identified its 1.2-kilobase RNA, which is not regulated by glucose repression. A 36-kilodalton SNF4 protein is predicted from

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O'Donnell, Allyson F., Rhonda R. McCartney, Dakshayini G. Chandrashekarappa, Bob B. Zhang, Jeremy Thorner та Martin C. Schmidt. "2-Deoxyglucose Impairs Saccharomyces cerevisiae Growth by Stimulating Snf1-Regulated and α-Arrestin-Mediated Trafficking of Hexose Transporters 1 and 3". Molecular and Cellular Biology 35, № 6 (2014): 939–55. http://dx.doi.org/10.1128/mcb.01183-14.

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The glucose analog 2-deoxyglucose (2DG) inhibits the growth ofSaccharomyces cerevisiaeand human tumor cells, but its modes of action have not been fully elucidated. Yeast cells lacking Snf1 (AMP-activated protein kinase) are hypersensitive to 2DG. Overexpression of either of two low-affinity, high-capacity glucose transporters, Hxt1 and Hxt3, suppresses the 2DG hypersensitivity ofsnf1Δ cells. The addition of 2DG or the loss of Snf1 reducesHXT1andHXT3expression levels and stimulates transporter endocytosis and degradation in the vacuole. 2DG-stimulated trafficking of Hxt1 and Hxt3 requires Rod1

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Madrigal-Perez, Luis Alberto, Gerardo M. Nava, Juan Carlos González-Hernández, and Minerva Ramos-Gomez. "Resveratrol increases glycolytic flux in Saccharomyces cerevisiae via a SNF1-dependet mechanism." Journal of Bioenergetics and Biomembranes 47, no. 4 (2015): 331–36. http://dx.doi.org/10.1007/s10863-015-9615-y.

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Charbon, Godefroid, Karin D. Breunig, Ruddy Wattiez, Jean Vandenhaute, and Isabelle Noël-Georis. "Key Role of Ser562/661 in Snf1-Dependent Regulation of Cat8p in Saccharomyces cerevisiae and Kluyveromyces lactis." Molecular and Cellular Biology 24, no. 10 (2004): 4083–91. http://dx.doi.org/10.1128/mcb.24.10.4083-4091.2004.

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ABSTRACT Utilization of nonfermentable carbon sources by Kluyveromyces lactis and Saccharomyces cerevisiae requires the Snf1p kinase and the Cat8p transcriptional activator, which binds to carbon source-responsive elements of target genes. We demonstrate that KlSnf1p and KlCat8p from K. lactis interact in a two-hybrid system and that the interaction is stronger with a kinase-dead mutant form of KlSnf1p. Of two putative phosphorylation sites in the KlCat8p sequence, serine 661 was identified as a key residue governing KlCat8p regulation. Serine 661 is located in the middle homology region, a re

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Celenza, J. L., F. J. Eng, and M. Carlson. "Molecular analysis of the SNF4 gene of Saccharomyces cerevisiae: evidence for physical association of the SNF4 protein with the SNF1 protein kinase." Molecular and Cellular Biology 9, no. 11 (1989): 5045–54. http://dx.doi.org/10.1128/mcb.9.11.5045.

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The SNF4 gene is required for expression of glucose-repressible genes in response to glucose deprivation in Saccharomyces cerevisiae. Previous evidence suggested that SNF4 is functionally related to SNF1, another essential gene in this global regulatory system that encodes a protein kinase. Increased SNF1 gene dosage partially compensates for a mutation in SNF4, and the SNF4 function is required for maximal SNF1 protein kinase activity in vitro. We have cloned SNF4 and identified its 1.2-kilobase RNA, which is not regulated by glucose repression. A 36-kilodalton SNF4 protein is predicted from

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Ferrer-Dalmau, Jofre, Francisca Randez-Gil, Maribel Marquina, José A. Prieto, and Antonio Casamayor. "Protein kinase Snf1 is involved in the proper regulation of the unfolded protein response in Saccharomyces cerevisiae." Biochemical Journal 468, no. 1 (2015): 33–47. http://dx.doi.org/10.1042/bj20140734.

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We show that Snf1, the yeast AMPK, affects the Ire1-RNase activity during the recovery phase of the UPR. Hence, our study suggests a connection between glucose availability and the UPR, identifying new targets for its regulation.

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Vincent, Olivier, Sergei Kuchin, Seung-Pyo Hong, Robert Townley, Valmik K. Vyas, and Marian Carlson. "Interaction of the Srb10 Kinase with Sip4, a Transcriptional Activator of Gluconeogenic Genes in Saccharomyces cerevisiae." Molecular and Cellular Biology 21, no. 17 (2001): 5790–96. http://dx.doi.org/10.1128/mcb.21.17.5790-5796.2001.

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ABSTRACT Sip4 is a Zn2Cys6 transcriptional activator that binds to the carbon source-responsive elements of gluconeogenic genes in Saccharomyces cerevisiae. The Snf1 protein kinase interacts with Sip4 and regulates its phosphorylation and activator function in response to glucose limitation; however, evidence suggested that another kinase also regulates Sip4. Here we examine the role of the Srb10 kinase, a component of the RNA polymerase II holoenzyme that has been primarily implicated in transcriptional repression but also positively regulates Gal4. We show that Srb10 is required for phosphor

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Nadal, Marina, Maria D. Garcia-Pedrajas, and Scott E. Gold. "The snf1 Gene of Ustilago maydis Acts as a Dual Regulator of Cell Wall Degrading Enzymes." Phytopathology® 100, no. 12 (2010): 1364–72. http://dx.doi.org/10.1094/phyto-01-10-0011.

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Many fungal plant pathogens are known to produce extracellular enzymes that degrade cell wall elements required for host penetration and infection. Due to gene redundancy, single gene deletions generally do not address the importance of these enzymes in pathogenicity. Cell wall degrading enzymes (CWDEs) in fungi are often subject to carbon catabolite repression at the transcriptional level such that, when glucose is available, CWDE-encoding genes, along with many other genes, are repressed. In Saccharomyces cerevisiae, one of the main players controlling this process is SNF1, which encodes a p

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Kaniak, Aneta, Zhixiong Xue, Daniel Macool, Jeong-Ho Kim, and Mark Johnston. "Regulatory Network Connecting Two Glucose Signal Transduction Pathways in Saccharomyces cerevisiae." Eukaryotic Cell 3, no. 1 (2004): 221–31. http://dx.doi.org/10.1128/ec.3.1.221-231.2004.

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ABSTRACT The yeast Saccharomyces cerevisiae senses glucose, its preferred carbon source, through multiple signal transduction pathways. In one pathway, glucose represses the expression of many genes through the Mig1 transcriptional repressor, which is regulated by the Snf1 protein kinase. In another pathway, glucose induces the expression of HXT genes encoding glucose transporters through two glucose sensors on the cell surface that generate an intracellular signal that affects function of the Rgt1 transcription factor. We profiled the yeast transcriptome to determine the range of genes target

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Salsaa, Michael, Kerestin Aziz, Pablo Lazcano, et al. "Valproate activates the Snf1 kinase in Saccharomyces cerevisiae by decreasing the cytosolic pH." Journal of Biological Chemistry 297, no. 4 (2021): 101110. http://dx.doi.org/10.1016/j.jbc.2021.101110.

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Tamai, K. T., X. Liu, P. Silar, T. Sosinowski, and D. J. Thiele. "Heat shock transcription factor activates yeast metallothionein gene expression in response to heat and glucose starvation via distinct signalling pathways." Molecular and Cellular Biology 14, no. 12 (1994): 8155–65. http://dx.doi.org/10.1128/mcb.14.12.8155-8165.1994.

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Metallothioneins constitute a class of low-molecular-weight, cysteine-rich metal-binding stress proteins which are biosynthetically regulated at the level of gene transcription in response to metals, hormones, cytokines, and other physiological and environmental stresses. In this report, we demonstrate that the Saccharomyces cerevisiae metallothionein gene, designated CUP1, is transcriptionally activated in response to heat shock and glucose starvation through the action of heat shock transcription factor (HSF) and a heat shock element located within the CUP1 promoter upstream regulatory regio

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Shinoda, Junro, and Yoshiko Kikuchi. "Rod1, an arrestin-related protein, is phosphorylated by Snf1-kinase in Saccharomyces cerevisiae." Biochemical and Biophysical Research Communications 364, no. 2 (2007): 258–63. http://dx.doi.org/10.1016/j.bbrc.2007.09.134.

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Schultz, J., L. Marshall-Carlson, and M. Carlson. "The N-terminal TPR region is the functional domain of SSN6, a nuclear phosphoprotein of Saccharomyces cerevisiae." Molecular and Cellular Biology 10, no. 9 (1990): 4744–56. http://dx.doi.org/10.1128/mcb.10.9.4744-4756.1990.

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The SSN6 protein functions as a negative regulator of a variety of genes in Saccharomyces cerevisiae and is required for normal growth, mating, and sporulation. It is a member of a family defined by a repeated amino acid sequence, the TPR (tetratricopeptide repeat) motif. Here, we have used specific antibody to identify and characterize the SSN6 protein. Both SSN6 and a bifunctional SSN6-beta-galactosidase fusion protein were localized in the nucleus by immunofluorescence staining. The N-terminal one-third of the protein containing the TPR units was identified as the region that is important f

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Silve, S., P. R. Rhode, B. Coll, J. Campbell, and R. O. Poyton. "ABF1 is a phosphoprotein and plays a role in carbon source control of COX6 transcription in Saccharomyces cerevisiae." Molecular and Cellular Biology 12, no. 9 (1992): 4197–208. http://dx.doi.org/10.1128/mcb.12.9.4197-4208.1992.

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Previously, we have shown that the Saccharomyces cerevisiae DNA-binding protein ABF1 exists in at least two different electrophoretic forms (K. S. Sweder, P. R. Rhode, and J. L. Campbell, J. Biol. Chem. 263: 17270-17277, 1988). In this report, we show that these forms represent different states of phosphorylation of ABF1 and that at least four different phosphorylation states can be resolved electrophoretically. The ratios of these states to one another differ according to growth conditions and carbon source. Phosphorylation of ABF1 is therefore a regulated process. In nitrogen-starved cells o

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Iida, H., S. Sakaguchi, Y. Yagawa, and Y. Anraku. "Cell cycle control by Ca2+ in Saccharomyces cerevisiae." Journal of Biological Chemistry 265, no. 34 (1990): 21216–22. http://dx.doi.org/10.1016/s0021-9258(17)45348-8.

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Duboc, P. "Physiology of Saccharomyces cerevisiae during cell cycle oscillations." Journal of Biotechnology 51, no. 1 (1996): 57–72. http://dx.doi.org/10.1016/0168-1656(96)01566-0.

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SRIENC, FRIEDRICH, and BRUCE S. DIEN. "Kinetics of the Cell Cycle of Saccharomyces cerevisiae." Annals of the New York Academy of Sciences 665, no. 1 Biochemical E (1992): 59–71. http://dx.doi.org/10.1111/j.1749-6632.1992.tb42574.x.

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Bogomolnaya, Lydia M., Ritu Pathak, Jinbai Guo, Roxhana Cham, Rodolfo Aramayo, and Michael Polymenis. "Hym1p affects cell cycle progression in Saccharomyces cerevisiae." Current Genetics 46, no. 4 (2004): 183–92. http://dx.doi.org/10.1007/s00294-004-0527-3.

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XU, Zhaojun, So-ichi YAGUCHI, and Kunio TSURUGI. "Gts1p stabilizes oscillations in energy metabolism by activating the transcription of TPS1 encoding trehalose-6-phosphate synthase 1 in the yeast Saccharomyces cerevisiae." Biochemical Journal 383, no. 1 (2004): 171–78. http://dx.doi.org/10.1042/bj20040967.

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We reported previously that Gts1p regulates oscillations of heat resistance in concert with those of energy metabolism in continuous cultures of the yeast Saccharomyces cerevisiae by inducing fluctuations in the levels of trehalose, but not in those of Hsp104 (heat shock protein 104). Further, the expression of TPS1, encoding trehalose-6-phosphate synthase 1, and HSP104 was activated by Gts1p in combination with Snf1 kinase, a transcriptional activator of glucose-repressible genes, in batch cultures under derepressed conditions. Here we show that, in continuous cultures, the mRNA level of TPS1

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