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Title 

Effect of a PMR1 disruption on the processing of heterologous glycoproteins secreted in the yeast Saccharomyces cerevisiae

Authors 

Moo Woong KimSu Min KoJeong Yoon KimJung Hoon SohnEui Sung ChoiHyun Ah KangSang Ki Rhee

Publisher 

Springer Verlag (Germany)

Issue Date 

2000

Citation 

Biotechnology and Bioprocess Engineering, vol. 5, no. 0, pp. 234-241

Keywords 

PMR1Saccharomyces cerevisiaesecretionglycosylationheterologous protein

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.

ISSN 

1226-8372

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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