Ontology highlight
ABSTRACT:
PROVIDER: PRJEB17688 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| ERR1720590_1.fastq.gz | Fastqsanger.gz | |||
| ERR1720590_2.fastq.gz | Fastqsanger.gz | |||
| ERR1720600_1.fastq.gz | Fastqsanger.gz | |||
| ERR1720600_2.fastq.gz | Fastqsanger.gz | |||
| ERR1720610_1.fastq.gz | Fastqsanger.gz |
Items per page: 5 1 - 5 of 62 |
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Project description:Transcriptional profiling of engineered yeast strains for protein secretion
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Project description:Saccharomyces cerevisiae has been used as a secretion host for production of various products, including pharmaceuticals. However, few antibody molecules have been functionally expressed in S. cerevisiae due to the incompatible surface glycosylation. Our laboratory previously isolated a group of yeast mutant strains with different α-amylase secretory capacities, and these evolved strains have showed advantages for production of some heterologous proteins. However, it is not known whether these secretory strains are generally suitable for pharmaceutical protein production. Here, three non-glycosylated antibody fragments with different configurations (Ran-Fab fragment Ranibizumab, Pex-the scFv peptide Pexelizumab, and Nan-a single V-type domain) were successfully expressed and secreted in three background strains with different secretory capacities, including HA (wild type), MA (evolved strain), and LA (evolved strain). However, the secretion of Ran and Nan were positively correlated with the strains’ secretory capacity, while Pex was most efficiently secreted in the parental strain. Therefore, transcriptional analysis was performed to explore the fundamental changes triggered by the expression of the different pharmaceutical proteins in these selected yeast strains.
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Project description:Transcriptome profiling of yeast strains responding to 0.7M NaCl treatment for 30 or 60 minutes. This study identified affected genes under both conditions tested. Transcript and protein changes were compared to determine mRNAs contribution to protein levels during salt acclimation.
2013-12-21 | GSE53549 | GEO
Project description:Protein secretion in yeast is a complex process and its efficiency depends on a variety of parameters. We performed a comparative proteome analysis of a set of Schizosaccharomyces pombe strains producing the alpha-glucosidase maltase in increasing amounts to investigate the overall proteomic response of the cell to the burden of protein production along the various steps of protein production and secretion. Proteome analysis of these strains, utilizing an isobaric labeling /two dimensional LC-MALDI MS approach, revealed complex changes, from chaperones and secretory transport machinery to proteins controlling transcription and translation. We also found an unexpectedly high amount of changes in enzyme levels of the central carbon metabolism and a significant upregulation of several amino acid biosyntheses. These amino acids were partially underrepresented in the cellular protein compared to the composition of the model protein. Additional feeding of these amino acids resulted in a 1.5-fold increase in protein secretion. Membrane fluidity was identified as a second bottleneck for high-level protein secretion and addition of fluconazole to the culture caused a significant decrease in ergosterol levels, while protein secretion could be further increased by a factor of 2.1. In summary, we show that high level protein secretion causes global changes of protein expression levels in the cell and that precursor availability and membrane composition limit protein secretion in this yeast. In this respect, comparative proteome analysis is a powerful tool to identify targets for an efficient increase of protein production and secretion in S. pombe. Additional supernatant analysis was performed using LC-ESI MS.
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Project description:This dataset contains additional experimental results for the determination of the effect of Fluconazole and amino acid supplementation to the NW10 strain of S. pombe. Protein secretion in yeast is a complex process and its efficiency depends on a variety of parameters. We performed a comparative proteome analysis of a set of Schizosaccharomyces pombe strains producing the alpha-glucosidase maltase in increasing amounts to investigate the overall proteomic response of the cell to the burden of protein production along the various steps of protein production and secretion. Proteome analysis of these strains, utilizing an isobaric labeling /two dimensional LC-MALDI MS approach, revealed complex changes, from chaperones and secretory transport machinery to proteins controlling transcription and translation. We also found an unexpectedly high amount of changes in enzyme levels of the central carbon metabolism and a significant upregulation of several amino acid biosyntheses. These amino acids were partially underrepresented in the cellular protein compared to the composition of the model protein. Additional feeding of these amino acids resulted in a 1.5-fold increase in protein secretion. Membrane fluidity was identified as a second bottleneck for high-level protein secretion and addition of fluconazole to the culture caused a significant decrease in ergosterol levels, while protein secretion could be further increased by a factor of 2.1. In summary, we show that high level protein secretion causes global changes of protein expression levels in the cell and that precursor availability and membrane composition limit protein secretion in this yeast. In this respect, comparative proteome analysis is a powerful tool to identify targets for an efficient increase of protein production and secretion in S. pombe. Additional supernatant analysis was performed using LC-ESI MS.
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Project description:Transcriptional profiling of anreuploid yeast strains grown in rich medium YEPD
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Project description:Transcriptional profiling of aneuploid yeast strains grown in rich medium YEPD
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