Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha

Cited 34 time in scopus
Metadata Downloads
Title
Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
Author(s)
Michael O Agaphonov; Anna N Packeiser; Maria B Chechenova; Eui Sung Choi; Michael D Ter-Avanesyan
Bibliographic Citation
Yeast, vol. 18, no. 5, pp. 391-402
Publication Year
2001
Abstract
A Hansenula polymorpha mutant with enhanced ability to secrete a heterologous protein has been isolated. The mutation defines a gene, designated OPU24, which encodes a protein highly homologous to GDP-mannose pyrophosphorylase Psa1p/Srb1p/Vig9p of Saccharomyces cerevisiae and CaSrb1p of Candida albicans. The opu24 mutant manifests phenotypes similar to those of S. cerevisiae mutants depleted for GDP-mannose, such as cell wall fragility and defects in N- and O-glycosylation of secreted proteins. The influence of the opu24 mutation on endoplasmic reticulum-associated protein degradation is discussed. The GenBank Accession No. for the OPU24 sequence is AF234177.
Keyword
cell wallhansenula polymorphaprotein glycosylationprotein secretionyeasturinary type plasminogen activator
ISSN
0749-503X
Publisher
Wiley
DOI
http://dx.doi.org/10.1002/yea.678
Type
Article
Appears in Collections:
Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.