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Title 

Essential role of YlMPO1, a novel Yarrowia lipolytica homologue of Saccharomyces cerevisiae MNN4, in mannosylphosphorylation of N- and O-linked glycans

Authors 

J N ParkY SongS A CheonOh Suk KwonDoo-Byoung OhY JigamiJ Y KimH A Kang

Publisher 

American Society for Microbiology

Issue Date 

2011

Citation 

Applied and Environmental Microbiology, vol. 77, no. 4, pp. 1187-1195

Keywords 

C terminusGene disruptionsGlycan structuresGlycansMolecular functionMutant strainNegative chargeO-GlycansO-linkedS.cerevisiaeSaccharomyces cerevisiaeSequence homologySugar moietyY. lipolyticaYarrowia lipolytica

Abstract 

Mannosylphosphorylation of N- and O-glycans, which confers negative charges on the surfaces of cells, requires the functions of both MNN4 and MNN6 in Saccharomyces cerevisiae. To identify genes relevant to mannosylphosphorylation in the dimorphic yeast Yarrowia lipolytica, the molecular functions of five Y. lipolytica genes showing significant sequence homology with S. cerevisiae MNN4 and MNN6 were investigated. A set of mutant strains in which Y. lipolytica MNN4 and MNN6 homologues were deleted underwent glycan structure analysis. In contrast to S. cerevisiae MNN4 (ScMNN4), the Y. lipolytica MNN4 homologue, MPO1 (YlMPO1), encodes a protein that lacks the long KKKKEEEE repeat domain at its C terminus. Moreover, just a single disruption of YlMPO1 resulted in complete disappearance of the acidic sugar moiety in both the N- and O-linked glycan profiles. In contrast, even quadruple disruption of all ScMNN6 homologues, designated YlKTR1, YlKTR2, YlKTR3, and YlKTR4, resulted in no apparent reduction in acidic sugar moieties. These findings strongly indicate that YlMpo1p performs a significant role in mannosylphosphorylation in Y. lipolytica with no involvement of the Mnn6p homologues. Mutant strains harboring the YlMPO1 gene disruption may serve as useful platforms for engineering Y. lipolytica glycosylation pathways for humanized glycans without any yeast-specific acidic modifications.

ISSN 

0099-2240

Link 

http://dx.doi.org/10.1128/AEM.02323-10

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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