Taxonomic group: fungi / Ascomycota
(Phylum: Ascomycota)
Organ / tissue: cell wall
NCBI PubMed ID: 21183647Publication DOI: 10.1128/AEM.02323-10Journal NLM ID: 7605801Publisher: American Society for Microbiology
Correspondence: Kim JY <jykim
cnu.ac.kr>, Kang HA <hyunkang
cau.ac.kr>
Institutions: Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan, Department of Life Science, Chung-Ang University, Seoul, South Korea, Integrative Omics Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, South Korea, Department of Microbiology and Molecular Biology, College of Bioscience and Biotechnology, Chungnam National University, Daejeon, South Korea, Research Center for Medical Glycoscience, National Institute of Advanced Industrial Science and Technology, Tsukuba, Japan.
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.
O-glycan, N-glycan, Saccharomyces cerevisiae, Yarrowia lipolytica, mannosylphosphorylation
Structure type: oligomer
Location inside paper: description for fig. 5, M2
Aglycon: (->3) L-Thr/L-Ser (protein)
Compound class: O-glycan
Contained glycoepitopes: IEDB_130701,IEDB_136104,IEDB_143632,IEDB_144983,IEDB_152206,IEDB_983930,SB_136,SB_196,SB_44,SB_67,SB_72
Methods: DNA techniques, acid hydrolysis, HPLC, enzymatic digestion, ion-exchange chromatography, capillary electrophoresis (CE), MALDI-TOF, CC
Related record ID(s): 43638, 43642, 43646, 43650, 43651, 43652
NCBI Taxonomy refs (TaxIDs): 4952Reference(s) to other database(s): GTC:G53402KW
Show glycosyltransferases
There is only one chemically distinct structure:
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