FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W4384070307> ?p ?o ?g. }

• W4384070307 abstract "Abstract The yeast Saccharomyces cerevisiae is widely used as a host cell for recombinant protein production due to its fast growth, cost-effective culturing, and ability to secrete large and complex proteins. However, one major drawback is the relatively low yield of produced proteins compared to other host systems. To address this issue, we developed an overlay assay to screen the yeast knockout collection and identify mutants that enhance recombinant protein production, specifically focusing on the secretion of the Trametes trogii fungal laccase enzyme. Gene ontology analysis of these mutants revealed an enrichment of processes including vacuolar targeting, vesicle trafficking, proteolysis, and glycolipid metabolism. We confirmed that a significant portion of these mutants also showed increased activity of the secreted laccase when grown in liquid culture. Notably, we found that the combination of deletions of OCA6 , a tyrosine phosphatase, along with PMT 1 or PMT2 , two ER membrane protein-O-mannosyltransferases involved in ER quality control, and SKI3 , a component of the SKI complex responsible for mRNA degradation, further increased secreted laccase activity. Conversely, we also identified over 200 gene deletions that resulted in decreased secreted laccase activity, including many genes that encode for mitochondrial proteins and components of the ER-associated degradation pathway. Intriguingly, the deletion of the ER DNAJ co-chaperone SCJ1 led to almost no secreted laccase activity. When we expressed SCJ1 from a low-copy plasmid, laccase secretion was restored. However, overexpression of Scj1p had a detrimental effect, indicating that precise dosing of key chaperone proteins is crucial for optimal recombinant protein expression. Importance Our study showcases a newly developed high throughput screening technique to identify yeast mutant strains that exhibit an enhanced capacity for recombinant protein production. Using a genome-wide approach, we show that vesicle trafficking plays a crucial role in protein production, as the genes associated with this process are notably enriched in our screen. Furthermore, we demonstrate that a specific set of gene deletions, which were not previously recognized for their impact on recombinant laccase production, can be effectively manipulated in combination to increase the production of heterologous proteins. This study offers potential strategies for enhancing the overall yield of recombinant proteins and provides new avenues for further research in optimizing protein production systems." @default.
• W4384070307 created "2023-07-13" @default.
• W4384070307 creator A5042454677 @default.
• W4384070307 creator A5046029600 @default.
• W4384070307 creator A5057099410 @default.
• W4384070307 creator A5060916439 @default.
• W4384070307 creator A5068495723 @default.
• W4384070307 creator A5069396293 @default.
• W4384070307 creator A5074493569 @default.
• W4384070307 creator A5092454266 @default.
• W4384070307 date "2023-07-10" @default.
• W4384070307 modified "2023-09-25" @default.
• W4384070307 title "Genome-wide screen identifies new set of genes for improved heterologous laccase expression in<i>Saccharomyces cerevisiae</i>" @default.
• W4384070307 cites W148128029 @default.
• W4384070307 cites W1589290041 @default.
• W4384070307 cites W1904777810 @default.
• W4384070307 cites W195389358 @default.
• W4384070307 cites W1966236299 @default.
• W4384070307 cites W1971498704 @default.
• W4384070307 cites W1982442422 @default.
• W4384070307 cites W1997859335 @default.
• W4384070307 cites W2009064016 @default.
• W4384070307 cites W2035792284 @default.
• W4384070307 cites W2038203729 @default.
• W4384070307 cites W2038591876 @default.
• W4384070307 cites W2038963685 @default.
• W4384070307 cites W2046995371 @default.
• W4384070307 cites W2049579702 @default.
• W4384070307 cites W2055792787 @default.
• W4384070307 cites W2056914971 @default.
• W4384070307 cites W2066533724 @default.
• W4384070307 cites W2077250786 @default.
• W4384070307 cites W2079810511 @default.
• W4384070307 cites W2083244640 @default.
• W4384070307 cites W2083274478 @default.
• W4384070307 cites W2107277218 @default.
• W4384070307 cites W2119783761 @default.
• W4384070307 cites W2123577912 @default.
• W4384070307 cites W2127073167 @default.
• W4384070307 cites W2127234401 @default.
• W4384070307 cites W2128021875 @default.
• W4384070307 cites W2128684741 @default.
• W4384070307 cites W2129288998 @default.
• W4384070307 cites W2130494754 @default.
• W4384070307 cites W2133197373 @default.
• W4384070307 cites W2139482843 @default.
• W4384070307 cites W2139577310 @default.
• W4384070307 cites W2139848107 @default.
• W4384070307 cites W2142437744 @default.
• W4384070307 cites W2142917513 @default.
• W4384070307 cites W2148020502 @default.
• W4384070307 cites W2151244582 @default.
• W4384070307 cites W2157734222 @default.
• W4384070307 cites W2236878792 @default.
• W4384070307 cites W2408236302 @default.
• W4384070307 cites W2528002330 @default.
• W4384070307 cites W2536468709 @default.
• W4384070307 cites W2605691915 @default.
• W4384070307 cites W2618782288 @default.
• W4384070307 cites W2621577344 @default.
• W4384070307 cites W2751313499 @default.
• W4384070307 cites W2768672147 @default.
• W4384070307 cites W2804829458 @default.
• W4384070307 cites W2944298841 @default.
• W4384070307 cites W3122485779 @default.
• W4384070307 cites W3137143246 @default.
• W4384070307 cites W3173903422 @default.
• W4384070307 cites W3187088979 @default.
• W4384070307 cites W4225607442 @default.
• W4384070307 cites W4281774287 @default.
• W4384070307 doi "https://doi.org/10.1101/2023.07.10.548373" @default.
• W4384070307 hasPublicationYear "2023" @default.
• W4384070307 type Work @default.
• W4384070307 citedByCount "0" @default.
• W4384070307 crossrefType "posted-content" @default.
• W4384070307 hasAuthorship W4384070307A5042454677 @default.
• W4384070307 hasAuthorship W4384070307A5046029600 @default.
• W4384070307 hasAuthorship W4384070307A5057099410 @default.
• W4384070307 hasAuthorship W4384070307A5060916439 @default.
• W4384070307 hasAuthorship W4384070307A5068495723 @default.
• W4384070307 hasAuthorship W4384070307A5069396293 @default.
• W4384070307 hasAuthorship W4384070307A5074493569 @default.
• W4384070307 hasAuthorship W4384070307A5092454266 @default.
• W4384070307 hasBestOaLocation W43840703071 @default.
• W4384070307 hasConcept C104317684 @default.
• W4384070307 hasConcept C108305142 @default.
• W4384070307 hasConcept C143065580 @default.
• W4384070307 hasConcept C181199279 @default.
• W4384070307 hasConcept C2777576037 @default.
• W4384070307 hasConcept C2779222958 @default.
• W4384070307 hasConcept C40767141 @default.
• W4384070307 hasConcept C49039625 @default.
• W4384070307 hasConcept C55493867 @default.
• W4384070307 hasConcept C76935637 @default.
• W4384070307 hasConcept C86803240 @default.
• W4384070307 hasConcept C95444343 @default.
• W4384070307 hasConceptScore W4384070307C104317684 @default.
• W4384070307 hasConceptScore W4384070307C108305142 @default.
• W4384070307 hasConceptScore W4384070307C143065580 @default.
• W4384070307 hasConceptScore W4384070307C181199279 @default.

• next