Kapteyn J C, Montijn R C, Vink E, de la Cruz J, Llobell A, Douwes J E, Shimoi H, Lipke P N, Klis F M
Institute of Molecular Cell Biology, BioCentrum Amsterdam, University of Amsterdam, The Netherlands.
Glycobiology. 1996 Apr;6(3):337-45. doi: 10.1093/glycob/6.3.337.
Yeast cell wall proteins, including Cwp1p and alpha-agglutinin, could be released by treating the cell wall with either beta-1,3-or beta-1,6-glucanases, indicating that both polymers are involved in anchoring cell wall proteins. It was shown immunologically that both beta-1,3- and beta-1,6-glucan were linked to yeast cell wall proteins, including Cwp1p and alpha-agglutinin. It was further shown that beta-1,3-glucan was linked to the wall protein through a beta-1,6-glucan moiety. The beta-1,6-glucan moiety could be removed from Cwp1p and other cell wall proteins by cleaving phosphodiester bridges either enzymatically using phosphodiesterases or chemically using ice-cold aqueous hydrofluoric acid. These observations are consistent with the notion that cell wall proteins in Saccharomyces cerevisiae are linked to a beta-1,3-/beta-1,6-glucan heteropolymer through a phosphodiester linkage and that this polymer is responsible for anchoring cell wall proteins. It is proposed that this polymer is identical to the alkali-soluble beta-1,3-/beta-1,6-glucan heteropolymer characterized by Fleet and Manners (1976, 1977).
酵母细胞壁蛋白，包括Cwp1p和α-凝集素，可以通过用β-1,3-或β-1,6-葡聚糖酶处理细胞壁来释放，这表明这两种聚合物都参与了细胞壁蛋白的锚定。免疫学研究表明，β-1,3-和β-1,6-葡聚糖都与酵母细胞壁蛋白相连，包括Cwp1p和α-凝集素。进一步研究表明，β-1,3-葡聚糖通过β-1,6-葡聚糖部分与壁蛋白相连。可以通过使用磷酸二酯酶酶切或使用冰冷的氢氟酸水溶液化学切割磷酸二酯桥，从Cwp1p和其他细胞壁蛋白中去除β-1,6-葡聚糖部分。这些观察结果与以下观点一致：酿酒酵母中的细胞壁蛋白通过磷酸二酯键与β-1,3-/β-1,6-葡聚糖杂聚物相连，并且这种聚合物负责锚定细胞壁蛋白。有人提出，这种聚合物与Fleet和Manners（1976年、1977年）所描述的碱溶性β-1,3-/β-1,6-葡聚糖杂聚物相同。
