Protein expression during lag phase and growth initiation in Saccharomyces cerevisiae

Brejning, Jeanette; Jespersen, Lene

doi:10.1016/s0168-1605(01)00726-7

Cited by 44 publications

(44 citation statements)

References 38 publications

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“…Differential expression of a number of identified proteins was not verified by gene expression results, demonstrating that other factors, besides levels of mRNA, had an influence on protein synthesis. Earlier studies (2,8) have reported the absence of correlation between expression patterns of the early induced proteins and the corresponding genes in other microorganisms.…”

Section: Discussionmentioning

confidence: 95%

“…bulgaricus showed that several proteins were strongly expressed in the lag phase, although only one protein (phosphoryl carrier protein HPr) was positively identified (30). Expression studies of Saccharomyces cerevisiae revealed about 20 proteins induced in the lag phase, which were primarily involved in protein synthesis, biosynthesis of amino acids, and carbohydrate metabolism (2,3). A recent transcriptional study of Bacillus licheniformis based on 250 DNA probes exposed at least 15 differentially expressed genes of diverse functions in the lag phase (14).…”

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confidence: 99%

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Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk

Larsen

Boye

Siegumfeldt

et al. 2006

Appl Environ Microbiol

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We investigated protein and gene expression in the lag phase of Lactococcus lactis subsp. lactis CNRZ 157 and compared it to the exponential and stationary phases. By means of two-dimensional polyacrylamide gel electrophoresis, 28 highly expressed lag-phase proteins, implicated in nucleotide metabolism, glycolysis, stress response, translation, transcription, cell division, amino acid metabolism, and coenzyme synthesis, were identified. Among the identified proteins, >2-fold induction and down-regulation in the lag phase were determined for 12 proteins in respect to the exponential phase and for 18 proteins in respect to the stationary phase. Transcriptional changes of the lag-phase proteins in L. lactis were studied by oligonucleotide microarrays. Good correlation between protein and gene expression studies was demonstrated for several differentially expressed proteins, including nucleotide biosynthetic enzymes, adenylosuccinate synthase (PurA), IMP dehydrogenase (GuaB), and aspartate carbamoyl transferase (PyrB); heat-shock protein DnaK; serine hydroxymethyl transferase (GlyA); carbon catabolite control protein (CcpA); elongation factor G (FusA); and cell division protein (FtsZ).Intracellular events occurring in bacteria just after introduction to a new environment provide the first evidence about physiological changes in the cells. When lactic acid bacteria are used as starter cultures, these intracellular changes may ensure a rapid prediction of the overall physiological status of the culture, which in turn defines the activity of the culture. Upon inoculation, the culture is exposed to massive environmental changes including nutrient availability, temperature, and pH. To adapt to new environments, bacteria have developed various metabolic responses. Recent research revealed a number of responses in Lactococcus lactis caused by exhaustion of essential nutrients such as purines (1), carbohydrates (7,18,36), and branched amino acids (10, 29), as well as responses to the temperature shift (6, 42), low pH (4,23,26,31), and a combination of these factors (13,25). However, only a few papers describe the intracellular changes occurring early in the cultivation upon transfer of the culture to a new rich medium. For example, proteomic research carried out with Lactobacillus delbrueckii subsp. bulgaricus showed that several proteins were strongly expressed in the lag phase, although only one protein (phosphoryl carrier protein HPr) was positively identified (30). Expression studies of Saccharomyces cerevisiae revealed about 20 proteins induced in the lag phase, which were primarily involved in protein synthesis, biosynthesis of amino acids, and carbohydrate metabolism (2, 3). A recent transcriptional study of Bacillus licheniformis based on 250 DNA probes exposed at least 15 differentially expressed genes of diverse functions in the lag phase (14).In this work, we investigated protein and gene expression in Lactococcus lactis subsp. lactis CNRZ 157 in the lag phase in comparison to the exponential and stationary growt...

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Section: Discussionmentioning

confidence: 95%

mentioning

confidence: 99%

Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk

Larsen

Boye

Siegumfeldt

et al. 2006

Appl Environ Microbiol

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“…In another study, Brejning et al (13,14) examined global changes in gene expression after resuspending cells that were post-diauxic (but not yet quiescent) in synthetic defined medium containing all essential nutrients. They focused on the lag VOL.…”

Section: Transcriptional Changesmentioning

confidence: 99%

“…However, the proteome has been monitored by two-dimensional gel electrophoresis during the lag phase on resuspension of post-diauxic shift cells in fresh synthetic complete medium (13). The overall rate of protein synthesis increased dramatically during the lag phase, with a concomitant increase in the number of proteins detectable on a single two-dimensional gel, from approximately 500 in early lag phase to 1,500 in late lag phase.…”

Section: Proteome Changesmentioning

confidence: 99%

“Sleeping Beauty”: Quiescence inSaccharomyces cerevisiae

Gray

Petsko

Johnston³

et al. 2004

Microbiol Mol Biol Rev

529

596

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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 properties of quiescent yeast cells, and clarify some definitions of the state. We propose that the processes by which a cell enters into, maintains viability in, and exits from quiescence are best viewed as an environmentally triggered cycle: the cell quiescence cycle. We synthesize what is known about the mechanisms by which yeast cells enter into quiescence, including the possible roles of the protein kinase A, TOR, protein kinase C, and Snf1p pathways. We also discuss selected mechanisms by which quiescent cells maintain viability, including metabolism, protein modification, and redox homeostasis. Finally, we outline what is known about the process by which cells exit from quiescence when nutrients again become available.

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“…Thus, knowledge of all biochemical pathways is of great importance relation to yeast physiology and performance in these industrial processes (1). Yeast proteases are involved in numerous biological functions, such as septum formation, sporulation, protein turnover, catabolite inactivation, enzyme secretion, and nutrition (10).…”

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confidence: 99%

Purification and Characterization of a Prolyl Aminopeptidase from Debaryomyces hansenii

Bolumar

Sanz

Aristoy

et al. 2003

Appl Environ Microbiol

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A prolyl aminopeptidase (PAP) (EC 3.4.11.5) was isolated from the cell extract of Debaryomyces hansenii CECT12487. The enzyme was purified by selective fractionation with protamine and ammonium sulfate, followed by two chromatography steps, which included gel filtration and anion-exchange chromatography. The PAP was purified 248-fold, with a recovery yield of 1.4%. The enzyme was active in a broad pH range (from 5 to 9.5), with pH and temperature optima at 7.5 and 45°C. The molecular mass was estimated to be around 370 kDa. The presence of inhibitors of serine and aspartic proteases, bestatin, puromycin, reducing agents, chelating agents, and different cations did not have any effect on the enzyme activity. Only iodoacetate, p-chloromercuribenzoic acid, and Hg 2؉ , which are inhibitors of cysteine proteases, markedly reduced the enzyme activity. The K m for proline-7-amido-4-methylcoumarin was 40 M. The enzyme exclusively hydrolyzed N-terminal-proline-containing substrates. This is the first report on the identification and purification of this type of aminopeptidase in yeast, which may contribute to the scarce knowledge about D. hansenii proteases and their possible roles in meat fermentation.

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Protein expression during lag phase and growth initiation in Saccharomyces cerevisiae

Cited by 44 publications

References 38 publications

Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk

Differential Expression of Proteins and Genes in the Lag Phase of Lactococcus lactis subsp. lactis Grown in Synthetic Medium and Reconstituted Skim Milk

“Sleeping Beauty”: Quiescence inSaccharomyces cerevisiae

Purification and Characterization of a Prolyl Aminopeptidase from Debaryomyces hansenii

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