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LIBRIS Formathandbok  (Information om MARC21)
FältnamnIndikatorerMetadata
00006637naa a2200817 4500
001oai:gup.ub.gu.se/302393
003SwePub
008240528s2020 | |||||||||||000 ||eng|
009oai:research.chalmers.se:4e367c4f-7925-479a-b961-e9f8da0d4985
0247 a https://gup.ub.gu.se/publication/3023932 URI
0247 a https://doi.org/10.1128/mBio.02743-202 DOI
0247 a https://research.chalmers.se/publication/5203912 URI
040 a (SwePub)gud (SwePub)cth
041 a eng
042 9 SwePub
072 7a ref2 swepub-contenttype
072 7a art2 swepub-publicationtype
1001 a Li, Feiran,d 1993u Novo Nordisk Fonden,Novo Nordisk Foundation,Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)feiranl
2451 0a Different routes of protein folding contribute to improved protein production in saccharomyces cerevisiae
264 1c 2020
520 a Protein folding is often considered the flux controlling process in protein synthesis and secretion. Here, two previously isolated Saccharomyces cerevisiae strains with increased α-amylase productivity were analyzed in chemostat cultures at different dilution rates using multi-omics data. Based on the analysis, we identified different routes of the protein folding pathway to improve protein production. In the first strain, the increased abundance of proteins working on the folding process, coordinated with upregulated glycogen metabolism and trehalose metabolism, helped increase α-amylase productivity 1.95-fold compared to the level in the original strain in chemostat culture at a dilution rate of 0.2/h. The second strain further strengthened the folding precision to improve protein production. More precise folding helps the cell improve protein production efficiency and reduce the expenditure of energy on the handling of misfolded proteins. As calculated using an enzyme-constrained genome-scale metabolic model, the second strain had an increased productivity of 2.36-fold with lower energy expenditure than that of the original under the same condition. Further study revealed that the regulation of N-glycans played an important role in the folding precision control and that overexpression of the glucosidase Cwh41p can significantly improve protein production, especially for the strains with improved folding ca-pacity but lower folding precision. Our findings elucidated in detail the mechanisms in two strains having improved protein productivity and thereby provided novel insights for industrial recombinant protein production as well as demonstrating how multi-omics analysis can be used for identification of novel strain-engineering targets. IMPORTANCE Protein folding plays an important role in protein maturation and se-cretion. In recombinant protein production, many studies have focused on the folding pathway to improve productivity. Here, we identified two different routes for improving protein production by yeast. We found that improving folding precision is a better strategy. Dysfunction of this process is also associated with several aberrant protein-associated human diseases. Here, our findings about the role of glucosidase Cwh41p in the precision control system and the characterization of the strain with a more precise folding process could contribute to the development of novel therapeutic strategies. © 2020 Qi et al.
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
650 7a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
650 7a NATURVETENSKAPx Biologix Mikrobiologi0 (SwePub)106062 hsv//swe
650 7a NATURAL SCIENCESx Biological Sciencesx Microbiology0 (SwePub)106062 hsv//eng
650 7a MEDICIN OCH HÄLSOVETENSKAPx Medicinsk bioteknologix Medicinsk bioteknologi0 (SwePub)304012 hsv//swe
650 7a MEDICAL AND HEALTH SCIENCESx Medical Biotechnologyx Medical Biotechnology0 (SwePub)304012 hsv//eng
653 a Constraint-based modeling
653 a Multi-omics analysis
653 a Protein folding precision
653 a Protein production
653 a Protein secretory pathway
653 a amylase
653 a Cwh41 protein
653 a glucosidase
653 a glycan
653 a recombinant protein
653 a unclassified drug
653 a Article
653 a control system
653 a controlled study
653 a energy expenditure
653 a glycogen metabolism
653 a metabolomics
653 a multiomics
653 a nonhuman
653 a priority journal
653 a protein folding
653 a protein glycosylation
653 a protein modification
653 a protein secretion
653 a protein synthesis
653 a proteomics
653 a Saccharomyces cerevisiae
653 a strain difference
653 a transcriptomics
653 a Multi-omics analysis
7001 a Yu, R.u Novo Nordisk Fonden,Novo Nordisk Foundation4 aut
7001 a Engqvist, Martin,d 1983u Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)marengq
7001 a Siewers, Verena,d 1976u Novo Nordisk Fonden,Novo Nordisk Foundation,Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)siewers
7001 a Fuchs, Johannesu Gothenburg University,Göteborgs universitet,Core Facilities, Proteomics,Core Facilities, Proteomics,University of Gothenburg4 aut0 (Swepub:gu)xfujoh
7001 a Nielsen, Jens B,d 1962u Danmarks Tekniske Universitet,Technical University of Denmark,Novo Nordisk Fonden,Novo Nordisk Foundation,BioInnovation Institute (BII),Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)nielsenj
7001 a Qi, Qi,d 1992u Novo Nordisk Fonden,Novo Nordisk Foundation,Chalmers tekniska högskola,Chalmers University of Technology4 aut0 (Swepub:cth)fomde
7102 a Novo Nordisk Fondenb Chalmers tekniska högskola4 org
7730 t mBiog 11:6, s. 1-12q 11:6<1-12x 2161-2129x 2150-7511
8564 u https://research.chalmers.se/publication/520391/file/520391_Fulltext.pdfx primaryx freey FULLTEXT
8564 8u https://gup.ub.gu.se/publication/302393
8564 8u https://doi.org/10.1128/mBio.02743-20
8564 8u https://research.chalmers.se/publication/520391

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