Cited 3 time in
- Effect of a PMR1 disruption on the processing of heterologous glycoproteins secreted in the yeast Saccharomyces cerevisiae
- Moo Woong Kim; Su Min Ko; Jeong Yoon Kim; Jung Hoon Sohn; Eui Sung Choi; Hyun Ah Kang; Sang Ki Rhee
- Bibliographic Citation
- Biotechnology and Bioprocess Engineering, vol. 5, pp. 234-241
- Publication Year
- 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.
- PMR1; Saccharomyces cerevisiae; secretion; glycosylation; heterologous protein
- South Korea
- Appears in Collections:
- Division of Biomaterials Research > Synthetic Biology and Bioengineering Research Center > 1. Journal Articles
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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