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Article: Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site

TitleEnhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site
Authors
Issue Date2013
PublisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action
Citation
PLoS One, 2013, v. 8 n. 9, p. e75347 How to Cite?
AbstractPichia pastoris is one of the most widely used expression systems for the production of recombinant secretory proteins. Its universal application is, however, somewhat hampered by its unpredictable yields for different heterologous proteins, which is now believed to be caused in part by their varied efficiencies to traffic through the host secretion machinery. The yeast endoprotease Kex2 removes the signal peptides from pre-proteins and releases the mature form of secreted proteins, thus, plays a pivotal role in the yeast secretory pathways. In this study, we found that the yields of many recombinant proteins were greatly influenced by Kex2 P1' site residues and the optimized P1's amino acid residue could largely determine the final amount of secretory proteins synthesized and secreted. A further improvement of secretory yield was achieved by genomic integration of additional Kex2 copies, which again highlighted the importance of Kex2 cleavage to the production of recombinant secretory proteins in Pichia yeast. © 2013 Yang et al.
Persistent Identifierhttp://hdl.handle.net/10722/194722
ISSN
2015 Impact Factor: 3.057
2015 SCImago Journal Rankings: 1.395
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorYang, Sen_US
dc.contributor.authorKuang, Yen_US
dc.contributor.authorLi, Hen_US
dc.contributor.authorLiu, Yen_US
dc.contributor.authorHui, Xen_US
dc.contributor.authorLi, Pen_US
dc.contributor.authorJiang, Zen_US
dc.contributor.authorZhou, Yen_US
dc.contributor.authorWang, Yen_US
dc.contributor.authorXu, Aen_US
dc.contributor.authorLi, Sen_US
dc.contributor.authorLiu, Pen_US
dc.contributor.authorWu, Den_US
dc.date.accessioned2014-02-17T02:04:41Z-
dc.date.available2014-02-17T02:04:41Z-
dc.date.issued2013en_US
dc.identifier.citationPLoS One, 2013, v. 8 n. 9, p. e75347en_US
dc.identifier.issn1932-6203-
dc.identifier.urihttp://hdl.handle.net/10722/194722-
dc.description.abstractPichia pastoris is one of the most widely used expression systems for the production of recombinant secretory proteins. Its universal application is, however, somewhat hampered by its unpredictable yields for different heterologous proteins, which is now believed to be caused in part by their varied efficiencies to traffic through the host secretion machinery. The yeast endoprotease Kex2 removes the signal peptides from pre-proteins and releases the mature form of secreted proteins, thus, plays a pivotal role in the yeast secretory pathways. In this study, we found that the yields of many recombinant proteins were greatly influenced by Kex2 P1' site residues and the optimized P1's amino acid residue could largely determine the final amount of secretory proteins synthesized and secreted. A further improvement of secretory yield was achieved by genomic integration of additional Kex2 copies, which again highlighted the importance of Kex2 cleavage to the production of recombinant secretory proteins in Pichia yeast. © 2013 Yang et al.-
dc.languageengen_US
dc.publisherPublic Library of Science. The Journal's web site is located at http://www.plosone.org/home.action-
dc.relation.ispartofPLoS Oneen_US
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleEnhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' siteen_US
dc.typeArticleen_US
dc.identifier.emailHui, X: hannahui@hkucc.hku.hken_US
dc.identifier.emailWang, Y: yuwanghk@hku.hken_US
dc.identifier.emailXu, A: amxu@hkucc.hku.hken_US
dc.identifier.authorityWang, Y=rp00239en_US
dc.identifier.authorityXu, A=rp00485en_US
dc.description.naturepublished_or_final_version-
dc.identifier.doi10.1371/journal.pone.0075347-
dc.identifier.pmid24069404-
dc.identifier.pmcidPMC3777899-
dc.identifier.scopuseid_2-s2.0-84884379098-
dc.identifier.hkuros227968en_US
dc.identifier.volume8en_US
dc.identifier.issue9-
dc.identifier.spagee75347en_US
dc.identifier.epagee75347en_US
dc.identifier.isiWOS:000324777300073-
dc.publisher.placeUnited States-

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