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- Publisher Website: 10.1371/journal.pone.0075347
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Article: Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site
Title | Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site |
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Authors | |
Issue Date | 2013 |
Publisher | Public 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? |
Abstract | Pichia 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 Identifier | http://hdl.handle.net/10722/194722 |
ISSN | 2023 Impact Factor: 2.9 2023 SCImago Journal Rankings: 0.839 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Yang, S | en_US |
dc.contributor.author | Kuang, Y | en_US |
dc.contributor.author | Li, H | en_US |
dc.contributor.author | Liu, Y | en_US |
dc.contributor.author | Hui, X | en_US |
dc.contributor.author | Li, P | en_US |
dc.contributor.author | Jiang, Z | en_US |
dc.contributor.author | Zhou, Y | en_US |
dc.contributor.author | Wang, Y | en_US |
dc.contributor.author | Xu, A | en_US |
dc.contributor.author | Li, S | en_US |
dc.contributor.author | Liu, P | en_US |
dc.contributor.author | Wu, D | en_US |
dc.date.accessioned | 2014-02-17T02:04:41Z | - |
dc.date.available | 2014-02-17T02:04:41Z | - |
dc.date.issued | 2013 | en_US |
dc.identifier.citation | PLoS One, 2013, v. 8 n. 9, p. e75347 | en_US |
dc.identifier.issn | 1932-6203 | - |
dc.identifier.uri | http://hdl.handle.net/10722/194722 | - |
dc.description.abstract | Pichia 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.language | eng | en_US |
dc.publisher | Public Library of Science. The Journal's web site is located at http://www.plosone.org/home.action | - |
dc.relation.ispartof | PLoS ONE | en_US |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Enhanced production of recombinant secretory proteins in Pichia pastoris by optimizing Kex2 P1' site | en_US |
dc.type | Article | en_US |
dc.identifier.email | Hui, X: hannahui@hkucc.hku.hk | en_US |
dc.identifier.email | Wang, Y: yuwanghk@hku.hk | en_US |
dc.identifier.email | Xu, A: amxu@hkucc.hku.hk | en_US |
dc.identifier.authority | Wang, Y=rp00239 | en_US |
dc.identifier.authority | Xu, A=rp00485 | en_US |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1371/journal.pone.0075347 | - |
dc.identifier.pmid | 24069404 | - |
dc.identifier.pmcid | PMC3777899 | - |
dc.identifier.scopus | eid_2-s2.0-84884379098 | - |
dc.identifier.hkuros | 227968 | en_US |
dc.identifier.volume | 8 | en_US |
dc.identifier.issue | 9 | - |
dc.identifier.spage | e75347 | en_US |
dc.identifier.epage | e75347 | en_US |
dc.identifier.isi | WOS:000324777300073 | - |
dc.publisher.place | United States | - |
dc.identifier.issnl | 1932-6203 | - |