Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
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- Mutation of the homologue of GDP-mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
- 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
- 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.
- cell wallhansenula polymorphaprotein glycosylationprotein secretionyeasturinary type plasminogen activator
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- Division of Bio Technology Innovation > BioProcess Engineering Center > 1. Journal Articles
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