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Soluble forms of YlCrh1p and YlCrh2p, cell wall proteins of Yarrowia lipolytica , have β‐1,3‐glycosidase activity
Author(s) -
Hwang JiSook,
Seo DongHyuck,
Kim JeongYoon
Publication year - 2006
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.1395
Subject(s) - yarrowia , glycoside hydrolase , biology , cell wall , biochemistry , saccharomyces cerevisiae , biosynthesis , hydrolase , mannosidase , enzyme , yeast
Crh1p and Crh2p of Saccharomyces cerevisiae are cell wall proteins covalently attached to cell wall glucan and are thought to be putative glycosidases involved in cell wall remodelling. We investigated whether YlCrh1p and YlCrh2p, the Yarrowia lipolytica proteins homologous to ScCrh1p and ScCrh2p, had the required glycosidase activity for cell wall biosynthesis and maintenance. Ylcrh1Δ and Ylcrh2Δ mutants showed sensitivity to compounds that interfere with cell wall construction. Soluble forms of YlCrh1p and YlCrh2p that lacked the C‐terminal consensus sequence for GPI anchoring showed glycosidase activity on laminarin, a substrate carrying β‐1,3‐glycosidic linkage. Our study suggests that the YlCrh1p and YlCrh2p may participate in cell wall biosynthesis and remodelling through their β‐1,3‐glycosidase activity. Copyright © 2006 John Wiley & Sons, Ltd.