@article{mbs:/content/journal/micro/10.1099/mic.0.26887-0, author = "Barnay-Verdier, Stéphanie and Boisramé, Anita and Beckerich, Jean-Marie", title = "Identification and characterization of two α-1,6-mannosyltransferases, Anl1p and Och1p, in the yeast Yarrowia lipolytica", journal= "Microbiology", year = "2004", volume = "150", number = "7", pages = "2185-2195", doi = "https://doi.org/10.1099/mic.0.26887-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.26887-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "ER, endoplasmic reticulum", keywords = "RST, random sequence tag", abstract = "In this study, the identification and characterization of the Yarrowia lipolytica homologues of Saccharomyces cerevisiae α-1,6-mannosyltransferases Anp1p and Och1p, designated YlAnl1p and YlOch1p, are described. In order to confirm the function of the Y. lipolytica proteins, including the previously isolated YlMnn9p, in the N-glycosylation pathway, a phenotypic analysis of the disrupted strains ΔYlmnn9, ΔYlanl1, ΔYloch1, ΔYlanl1ΔYlmnn9 and ΔYlmnn9ΔYloch1 was performed. Disruption of the YlMNN9, YlANL1 and YlOCH1 genes caused an increased sensitivity to SDS, compatible with a glycosylation defect, and to Calcofluor White, characteristic of cell-wall defects. Moreover, Western-blot analysis of a heterologous glycosylated protein confirmed a direct role of YlMnn9p and YlAnl1p in the N-glycosylation process. These mutant strains, ΔYlmnn9, ΔYlanl1, ΔYloch1, ΔYlanl1ΔYlmnn9 and ΔYlmnn9ΔYloch1 may thus be used to establish a model for the Y. lipolytica N-linked glycosylation pathway.", }