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    Yeast. 2001 Mar 30;18(5):391-402.

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

    Agaphonov MO, Packeiser AN, Chechenova MB, Choi ES, Ter-Avanesyan MD.

    Institute of Experimental Cardiology, Cardiology Research Centre, 3rd Cherepkovskaya Street 15A, Moscow 121552, Russia. molgen@cardio.ru

    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.

    PMID: 11255248 [PubMed - indexed for MEDLINE]

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