Effect of a PMR1 Disruption on the Processing of Heterologous Glycoproteins Secreted in the Yeast Saccharomyces cerevisiae
DC Field | Value | Language |
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dc.contributor.author | Kim, Moo Woong | - |
dc.contributor.author | Ko, Su-Min | - |
dc.contributor.author | Kim, Jeong-Yoon | - |
dc.contributor.author | Sohn, Jung-Hoon | - |
dc.contributor.author | Choi, Eui-Sung | - |
dc.contributor.author | Kang, Hyun Ah | - |
dc.contributor.author | Rhee, Sang-Ki | - |
dc.date.accessioned | 2022-05-11T02:40:38Z | - |
dc.date.available | 2022-05-11T02:40:38Z | - |
dc.date.issued | 2000-08 | - |
dc.identifier.issn | 1226-8372 | - |
dc.identifier.issn | 1976-3816 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57525 | - |
dc.description.abstract | The Saccharomyces cerevisiae PMR1 gene encodes a Ca2+-ATPase localized in the Golgi. We have investigated the effects of PMR1 disruption in S. cerevisiae on the glycosylation and secretion of three heterologous glycoproteins, human α1-antitrypsin (α1,-AT), human antithrombin III (ATHIII), and Aspergillus niger glucose oxidase (GOD). The pmr1 null mutant strain secreted larger amounts of ATHIII and GOD proteins per a unit cell mass than the wild type strain. Despite a lower growth rate of the pmr1 mutant, two-fold higher level of human ATHIII was detected in the culture supernatant from the pmr1 mutant compared to that of the wild-type strain. The pmr1 mutant strain secreted α1-AT and the GOD proteins mostly as core-glycosylated forms, in contrast to the hyperglycosylated proteins secreted in the wild-type strain. Furthermore, the core-glycosylated forms secreted in the pmr1 mutant migrated slightly faster on SDS-PAGE than those secreted in the mnn9 deletion mutant and the wild type strains. Analysis of the recombinant GOD with anti-α,3-mannose antibody revealed that GOD secreted in the pmr1 mutant did not have terminal α1,3-linked mannoses unlike those secreted in the mnn9 mutant and the wild type strains. The present results indicate that the pmr1 mutant, with the super-secretion phenotype, is useful as a host system to produce recombinant glycoproteins lacking high-mannose outer chains. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Korean Society for Biotechnology and Bioengineering | - |
dc.title | Effect of a PMR1 Disruption on the Processing of Heterologous Glycoproteins Secreted in the Yeast Saccharomyces cerevisiae | - |
dc.type | Article | - |
dc.identifier.doi | 10.1007/BF02942179 | - |
dc.identifier.bibliographicCitation | Biotechnology and Bioprocess Engineering, v.5, no.4, pp 234 - 241 | - |
dc.description.isOpenAccess | Y | - |
dc.identifier.scopusid | 2-s2.0-0000881141 | - |
dc.citation.endPage | 241 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 234 | - |
dc.citation.title | Biotechnology and Bioprocess Engineering | - |
dc.citation.volume | 5 | - |
dc.type.docType | Article | - |
dc.publisher.location | 대한민국 | - |
dc.subject.keywordAuthor | Glycosylation | - |
dc.subject.keywordAuthor | Heterologous protein | - |
dc.subject.keywordAuthor | PMR1 | - |
dc.subject.keywordAuthor | Saccharomyces cerevisiae | - |
dc.subject.keywordAuthor | Secretion | - |
dc.description.journalRegisteredClass | scopus | - |
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