Effect of a PMR1 Disruption on the Processing of Heterologous Glycoproteins Secreted in the Yeast Saccharomyces cerevisiaeopen access
- Authors
- Kim, Moo Woong; Ko, Su-Min; Kim, Jeong-Yoon; Sohn, Jung-Hoon; Choi, Eui-Sung; Kang, Hyun Ah; Rhee, Sang-Ki
- Issue Date
- Aug-2000
- Publisher
- Korean Society for Biotechnology and Bioengineering
- Keywords
- Glycosylation; Heterologous protein; PMR1; Saccharomyces cerevisiae; Secretion
- Citation
- Biotechnology and Bioprocess Engineering, v.5, no.4, pp 234 - 241
- Pages
- 8
- Journal Title
- Biotechnology and Bioprocess Engineering
- Volume
- 5
- Number
- 4
- Start Page
- 234
- End Page
- 241
- URI
- https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/57525
- DOI
- 10.1007/BF02942179
- ISSN
- 1226-8372
1976-3816
- 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.
- Files in This Item
-
- Appears in
Collections - College of Natural Sciences > Department of Life Science > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.