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Mutation of the homologue of GDP‐mannose pyrophosphorylase alters cell wall structure, protein glycosylation and secretion in Hansenula polymorpha
Author(s) -
Agaphonov Michael O.,
Packeiser An.,
Chechenova Maria B.,
Choi EuiSung,
TerAvanesyan Michael D.
Publication year - 2001
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.678
Subject(s) - biology , mannose , mutant , glycosylation , saccharomyces cerevisiae , secretion , mutation , endoplasmic reticulum , secretory pathway , heterologous , biochemistry , gene , golgi apparatus
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. Copyright © 2001 John Wiley & Sons, Ltd.