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酿酒酵母细胞壁中嵌合蛋白的糖基化作用。

Glucosylation of chimeric proteins in the cell wall of Saccharomyces cerevisiae.

作者信息

van Berkel M A, Caro L H, Montijn R C, Klis F M

机构信息

Institute for Molecular Cell Biology, University of Amsterdam, BioCentrum Amsterdam, The Netherlands.

出版信息

FEBS Lett. 1994 Jul 25;349(1):135-8. doi: 10.1016/0014-5793(94)00631-8.

Abstract

Extension of a reporter protein with the carboxyterminal thirty amino acids of the cell wall mannoprotein alpha-agglutinin of Saccharomyces cerevisiae resulted in incorporation of the chimeric protein in the cell wall. By Western analysis it was shown that the incorporated protein contained beta-1,6-glucan similar to endogenous cell wall proteins, whereas excreted reporter protein was not glucosylated. This suggests that beta-1,6-glucan is involved in anchoring mannoproteins in the cell wall.

摘要

用酿酒酵母细胞壁甘露糖蛋白α-凝集素的羧基末端30个氨基酸对报告蛋白进行延伸,导致嵌合蛋白整合到细胞壁中。通过蛋白质免疫印迹分析表明,整合的蛋白含有与内源性细胞壁蛋白相似的β-1,6-葡聚糖,而分泌的报告蛋白未被糖基化。这表明β-1,6-葡聚糖参与了甘露糖蛋白在细胞壁中的锚定。

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