The Cln3 cyclin is down-regulated by translational repression and degradation during the G1 arrest caused by nitrogen deprivation in budding yeast

Gallego, Carme; Garí, Eloi; Colomina, Neus; Herrero, Enrique; Aldea, Martí

doi:10.1093/emboj/16.23.7196

Cited by 163 publications

(200 citation statements)

References 59 publications

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“…BY4741 WHI5::GFP 57 (supplied by Invitrogen) and CML128 (a S288C derivative 58 ) were used as wild-type strains of Saccharomyces cerevisiae. Standard PCR-based gene-replacement methods were used to obtain the indicated deletions, C-terminal translational fusions to GFP and mCherry, or transcriptional fusions to the GAL1 promoter at the respective chromosomal loci.…”

Section: Methodsmentioning

confidence: 99%

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

et al. 2012

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Budding yeast cells are assumed to trigger start and enter the cell cycle only after they attain a critical size set by external conditions. However, arguing against deterministic models of cell size control, cell volume at start displays great individual variability even under constant conditions. Here we show that cell size at start is robustly set at a single-cell level by the volume growth rate in G1, which explains the observed variability. We find that this growth-rate-dependent sizer is intimately hardwired into the start network and the Ydj1 chaperone is key for setting cell size as a function of the individual growth rate. mathematical modelling and experimental data indicate that a growth-rate-dependent sizer is sufficient to ensure size homeostasis and, as a remarkable advantage over a rigid sizer mechanism, it reduces noise in G1 length and provides an immediate solution for size adaptation to external conditions at a population level.

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Section: Methodsmentioning

confidence: 99%

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

et al. 2012

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“…Organisms and Culture Conditions-The strain used throughout this work was Saccharomyces cerevisiae CML128 (25). Yeast cells were grown in rich YPD medium (1% yeast extract, 2% peptone, 2% glucose) or under calorie restriction (YPD medium with 0.5% glucose) by incubation in a rotary shaker at 30°C.…”

Section: Methodsmentioning

confidence: 99%

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

Reverter-Branchat

Cabiscol

Tamarit

et al. 2004

Journal of Biological Chemistry

194

168

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Oxidative modifications of cellular components have been described as one of the main contributions to aged phenotype. In Saccharomyces cerevisiae, two distinct life spans can be considered, replicative and chronological. The relationship between both aging models is still not clear despite suggestions that these phenomena may be related. In this work, we show that replicative and chronological-aged yeast cells are affected by an oxidative stress situation demonstrated by increased protein carbonylation when compared with young cells. The data on the identification of these oxidatively modified proteins gives clues to better understand cellular dysfunction that occurs during aging. Strikingly, although in both aging models metabolic differences are important, major targets are almost the same. Common targets include stress resistance proteins (Hsp60 and Hsp70) and enzymes involved in glucose metabolism such as enolase, glyceraldehydes-3-P dehydrogenase, fructose-1,6-biphosphate aldolase, pyruvate decarboxylase, and alcohol dehydrogenase. In both aging models, calorie restriction results in decreased damage to these proteins. In addition, chronological-aged cells grown under glucose restriction displayed lowered levels of lipid peroxidation product lipofuscin. Intracellular iron concentration is kept almost unchanged, whereas in non-restricted cells, the values increase up 4 -5 times. The pro-oxidant effects of such increased iron concentration would account for the damage observed. Also, calorie-restricted cells show undamaged catalase, which clearly appears carbonylated in cells grown at a high glucose concentration. These results may explain lengthening of the viability of chronological-aged cells and could have an important role in replicative life span extension by calorie restriction.

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“…A putative regulator of yeast eIF4E function, termed Eap1p (eIF4E-associated protein 1), may also be involved in this process, as disruption of the EAP1 gene results in partial rapamycin resistance (53). The G 1 arrest in response to Tor inactivation was suggested to be due to the inhibition of translation of an mRNA coding for a cyclin involved in G 1 to S progression, CLN3, because the cell cycle block can be overcome by forced expression of CLN3 (54)(55)(56). 59).…”

Section: Tor Signaling Modulates the Phosphorylation State Of Proteinmentioning

confidence: 99%

The target of rapamycin (TOR) proteins

Raught

Gingras

Sonenberg

2001

Proc. Natl. Acad. Sci. U.S.A.

556

437

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Rapamycin potently inhibits downstream signaling from the target of rapamycin (TOR) proteins. These evolutionarily conserved protein kinases coordinate the balance between protein synthesis and protein degradation in response to nutrient quality and quantity. The TOR proteins regulate (i) the initiation and elongation phases of translation, (ii) ribosome biosynthesis, (iii) amino acid import, (iv) the transcription of numerous enzymes involved in multiple metabolic pathways, and (v) autophagy. Intriguingly, recent studies have also suggested that TOR signaling plays a critical role in brain development, learning, and memory formation. Rapamycin Inhibits Long-Term FacilitationS ynaptic plasticity, the capacity of neurons to modulate the strength of synaptic connections, is believed to be critical for learning and memory formation. Long-term synaptic plasticity (necessary for the formation of long-term memory) requires alterations in gene expression and the establishment of new synaptic connections (1-3). These findings presented an interesting dilemma: That is, how can changes in gene expression in the cell body alter the strength of individual synaptic connections? Recent data suggest that stimulated synapses are ''tagged'' to capture mRNAs produced in the soma and exported throughout the cell (4). Synaptic tagging thus results in localization of mRNAs only to those synapses marked by previous activity. This model also presupposes that long-term plasticity depends on local translation of the localized mRNAs. Indeed, ribosomes, tRNAs, translation initiation factors, and translation elongation factors are found in dendrites (5, 6), and protein synthesis has been demonstrated to occur in isolated synaptic bodies (7,8). Functional studies have demonstrated that protein synthesis is required for potentiation of synaptic transmission elicited by neurotrophic factors in hippocampal slices (9), and for the establishment of long-term facilitation in Aplysia neurons (10). Kandel and coworkers implicated a specific intracellular signaling pathway in this process by demonstrating that serotoninstimulated synaptic protein synthesis can be blocked with rapa-

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The Cln3 cyclin is down-regulated by translational repression and degradation during the G1 arrest caused by nitrogen deprivation in budding yeast

Cited by 163 publications

References 59 publications

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

The critical size is set at a single-cell level by growth rate to attain homeostasis and adaptation

Oxidative Damage to Specific Proteins in Replicative and Chronological-aged Saccharomyces cerevisiae

The target of rapamycin (TOR) proteins

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