Production of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins

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dc.contributor.authorMi-Jin Kim-
dc.contributor.authorBong Hyun Sung-
dc.contributor.authorH J Kim-
dc.contributor.authorJung Hoon Sohn-
dc.contributor.authorJung Hoon Bae-
dc.date.accessioned2022-10-26T16:32:23Z-
dc.date.available2022-10-26T16:32:23Z-
dc.date.issued2022-
dc.identifier.issn0175-7598-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/30508-
dc.description.abstractProtein expression with a fusion partner followed by the removal of the fusion partner via in vitro processing with a specific endoprotease is a favored method for the efficient production of intact recombinant proteins. Due to the high cost of commercial endoproteases, this process is restricted to laboratories. Kex2p is a membrane-bound serine protease that cleaves after dibasic residues of substrates in the late Golgi network. Although Kex2p is a very efficient endoprotease with exceptional specificity, it has not yet been used for the in vitro processing of fusion proteins due to its autolysis and high production cost. In this study, we developed an alternative endoprotease, autolysis-proof Kex2p, via site-directed mutagenesis of truncated KEX2 from Candida albicans (CaKEX2). Secretory production of manipulated CaKex2p was improved by employing target protein-specific translational fusion partner in Saccharomyces cerevisiae. The mass production of autolysis-proof Kex2p could facilitate the use of Kex2p for the large-scale production of recombinant proteins. KEY POINTS: ? A soluble and active CaKex2p variant was produced by autocatalytic cleavage of the pro-peptide after truncation of C-terminus ? Autolysis-proof CaKex2p was developed by site-directed mutagenesis ? Secretion of autolysis-proof CaKex2p was improved by employing optimal translational fusion partner in Saccharomyces cerevisiae.-
dc.publisherSpringer-
dc.titleProduction of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins-
dc.title.alternativeProduction of autolysis-proof Kex2 protease from Candida albicans in Saccharomyces cerevisiae for in vitro processing of fusion proteins-
dc.typeArticle-
dc.citation.titleApplied Microbiology and Biotechnology-
dc.citation.number21-
dc.citation.endPage7072-
dc.citation.startPage7063-
dc.citation.volume106-
dc.contributor.affiliatedAuthorMi-Jin Kim-
dc.contributor.affiliatedAuthorBong Hyun Sung-
dc.contributor.affiliatedAuthorJung Hoon Sohn-
dc.contributor.affiliatedAuthorJung Hoon Bae-
dc.contributor.alternativeName김미진-
dc.contributor.alternativeName성봉현-
dc.contributor.alternativeName김현진-
dc.contributor.alternativeName손정훈-
dc.contributor.alternativeName배정훈-
dc.identifier.bibliographicCitationApplied Microbiology and Biotechnology, vol. 106, no. 21, pp. 7063-7072-
dc.identifier.doi10.1007/s00253-022-12212-6-
dc.subject.keywordKEX2-
dc.subject.keywordCandida albicans-
dc.subject.keywordSecretion-
dc.subject.keywordSaccharomyces cerevisiae-
dc.subject.keywordAutolysis-proof-
dc.subject.localCandida albicans-
dc.subject.localcandida albicans-
dc.subject.localSecretion-
dc.subject.localsecretion-
dc.subject.localSaccharomyces cerevisiae-
dc.subject.localsaccharomyces cerevisiae-
dc.description.journalClassY-
Appears in Collections:
Synthetic Biology and Bioengineering Research Institute > Synthetic Biology Research Center > 1. Journal Articles
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