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

FEBS Letters

M. Hernández, Luis¹  Mañas, Paula¹  Olivero, Isabel¹ 

[1] Department of Microbiology, University of Extremadura, 06071 Badajoz, Spain

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;   

DOI  :  10.1016/S0014-5793(00)01635-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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.

【 授权许可】

Unknown