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首页> 外文期刊>Molecular and Cellular Biology >A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin.
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A pathway for cell wall anchorage of Saccharomyces cerevisiae alpha-agglutinin.

机译：酿酒酵母α-凝集素的细胞壁锚定的途径。

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摘要

Saccharomyces cerevisiae alpha-agglutinin is a cell wall-anchored adhesion glycoprotein. The previously identified 140-kDa form, which contains a glycosyl-phosphatidylinositol (GPI) anchor (D. Wojciechowicz, C.-F. Lu, J. Kurjan, and P. N. Lipke, Mol. Cell. Biol. 13:2554-2563, 1993), and additional forms of 80, 150, 250 to 300, and > 300 kDa had the properties of intermediates in a transport and cell wall anchorage pathway. N glycosylation and additional modifications resulted in successive increases in size during transport. The 150- and 250- to 300-kDa forms were membrane associated and are likely to be intermediates between the 140-kDa form and a cell surface GPI-anchored form of > 300 kDa. A soluble form of > 300 kDa that lacked the GPI anchor had properties of a periplasmic intermediate between the plasma membrane form and the > 300-kDa cell wall-anchored form. These results constitute experimental support for the hypothesis that GPI anchors act to localize alpha-agglutinin to the plasma membrane and that cell wall anchorage involves release from the GPI anchor to produce a periplasmic intermediate followed by linkage to the cell wall.
机译：酿酒酵母α-凝集素是细胞壁锚定的粘附糖蛋白。先前确定的140 kDa形式，其中包含糖基磷脂酰肌醇（GPI）锚点（D. Wojciechowicz，C.-F. Lu，J. Kurjan和PN Lipke，Mol。Cell。Biol。13：2554-2563， （1993），以及80、150、250至300和> 300 kDa的其他形式具有转运和细胞壁锚定途径中的中间体的性质。 N糖基化和其他修饰导致在运输过程中大小连续增加。 150 kDa和250 kDa到300 kDa的形式与膜相关，可能是140 kDa形式和细胞表面GPI锚定形式> 300 kDa的中间产物。缺少GPI锚的> 300 kDa的可溶形式具有质膜形式与> 300 kDa细胞壁锚定形式之间的周质中间物的特性。这些结果为以下假设提供了实验支持：GPI锚可将α-凝集素定位于质膜，而细胞壁的锚固则涉及从GPI锚释放以产生周质中间体，然后连接至细胞壁。

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