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酿酒酵母细胞壁蛋白含β-1,6-葡聚糖的侧链与糖基磷脂酰肌醇(GPI)部分的聚糖核心相连。

The beta-1, 6-glucan containing side-chain of cell wall proteins of Saccharomyces cerevisiae is bound to the glycan core of the GPI moiety.

作者信息

Van Der Vaart J M, te Biesebeke R, Chapman J W, Klis F M, Verrips C T

机构信息

Department of Molecular Cell Biology, University of Utrecht, The Netherlands.

出版信息

FEMS Microbiol Lett. 1996 Dec 15;145(3):401-7. doi: 10.1111/j.1574-6968.1996.tb08607.x.

Abstract

Cell wall proteins of Saccharomyces cerevisiae are anchored by means of a beta-1, 6-glucan-containing side-chain. It is not known whether this chain is linked to the protein part (e.g. through carbohydrate side-chains) or to the glycosylphosphatidylinositol (GPI) moiety of cell wall proteins. An IgA protease recognition site was introduced in Cwp2p, a beta-1, 6-glucosylated cell wall protein, immediately N-terminal from the omega amino acid (the attachment site of the GPI moiety). Proteolytic cleavage of this site revealed that the beta-1, 6-glucan epitope was not linked to the protein part. We conclude that neither N-or O-glycosylation is involved in beta-glucosylation of cell wall proteins. This confirms that the glycan core of the GPI moiety is the probable beta-1, 6-glucan attachment site.

摘要

酿酒酵母的细胞壁蛋白通过含β-1,6-葡聚糖的侧链进行锚定。目前尚不清楚该链是与蛋白质部分相连(例如通过碳水化合物侧链)还是与细胞壁蛋白的糖基磷脂酰肌醇(GPI)部分相连。在Cwp2p(一种β-1,6-糖基化的细胞壁蛋白)中,紧挨着ω氨基酸(GPI部分的附着位点)的N端引入了一个IgA蛋白酶识别位点。该位点的蛋白水解切割表明,β-1,6-葡聚糖表位不与蛋白质部分相连。我们得出结论,N-糖基化或O-糖基化均不参与细胞壁蛋白的β-糖基化。这证实了GPI部分的聚糖核心可能是β-1,6-葡聚糖的附着位点。

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