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The mnn2 mutant of Saccharomyces cerevisiae is affected in phosphorylation of N‐linked oligosaccharides
[摘要]

We studied the phosphorylation of the inner core region of N-linked oligosaccharides in the mannan defective mutant Saccharomyces cerevisiae mnn2 which was described as unable to synthesize branches on the outer chain. We performed structural studies of the N-oligosaccharides synthesized by the strains mnn2, mnn1mnn2mnn9 and mnn1mnn9ldb8, and the results are compared with previously published structural data of mnn1mnn2mnn10 and mnn1mnn9 [Hernández, L.M., Ballou, L., Alvarado, E., Tsai, P.-K. and Ballou, C.E. (1989) J. Biol. Chem. 264, 13648–13659]. We conclude that the mnn2/ldb8 mutation is responsible for the inhibition of incorporation of phosphate to mannose A3 (see below), a particular phosphorylation site of the inner core, while phosphorylation at the other possible site (mannose C1) is allowed, although it is also reduced. *Phosphorylation sites in mnn1mnn9.

[发布日期]  [发布机构] 
[效力级别]  [学科分类] 生物化学/生物物理
[关键词] Phosphorylation;N-Oligosaccharide;mnn2;Saccharomyces cerevisiae;endo H;endo β-N-acetylglucosaminidase;1H-NMR;1H-nuclear magnetic resonance;MAPK;mitogen-activated protein kinase [时效性] 
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