Protein O-Glycosylation in Fungi : Diverse Structures and Multiple Functions
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概要
- 論文の詳細を見る
Protein glycosylation is essential for eukaryotic cells from yeasts to humans. When compared to N-glycosylation, O-glycosylation is variable in sugar components and the mode of linkages connecting the sugars. In fungi, secretory proteins are commonly mannosylated by protein O-mannosyltransferase (PMT) in the endoplasmic reticulum, and subsequently glycosylated by several glycosyltransferases in the Golgi apparatus to form glycoproteins with diverse O-glycan structures. Protein O-glycosylation has roles in modulating the function of secretory proteins by enhancing the stability and solubility of the proteins, by affording protection from protease degradation, and by acting as a sorting determinant in yeasts. In filamentous fungi, protein O-glycosylation contributes to proper maintenance of fungal morphology, hyphal development, and differentiation. This review describes recent studies of the structure and function of protein O-glycosylation in industrially and medically important fungi.
- 社団法人 日本農芸化学会の論文
- 2007-06-23
著者
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GOTO Masatoshi
Department of Agricultural Chemistry, Kyushu University
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Goto Masatoshi
Department Of Agricultural Chemistry Kyushu University
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Goto Masatoshi
Department Of Bioscience And Biotechnology Faculty Of Agriculture Kyushu University
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