Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus
Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus
复制标题
DOI：
10.1099/00221287-148-9-2819
复制
发表时间：
2002-09-01
期刊：
影响因子：
2.8
通讯作者：
Latgé, JP
中科院分区：
文献类型：
--
作者：
Bernard, M;Mouyna, I;Latgé, JP
在丝状真菌烟曲霉中，绝大多数细胞壁相关蛋白是在细胞壁中转运的分泌蛋白。这些蛋白质可被去污剂和还原剂溶解。SDS/β-巯基乙醇处理的细胞壁提取物与水解细胞壁多糖的各种重组酶的孵育导致仅在1，3-β-葡聚糖酶存在下孵育细胞壁后以微量释放独特的蛋白质。序列分析和生物化学研究表明，这种糖蛋白，具有80 kDa的表观分子量，是一种酸性磷酸酶（PhoAp），磷酸单酯和磷酸二酯的活性。PhoAp是一种糖基磷脂酰肌醇锚定的蛋白质，其在A的培养滤液和细胞壁部分中回收。烟曲霉在其锚分裂后。它也是一种磷酸盐抑制性酸性磷酸酶。在富含磷酸盐的培养基中，PhoAp的缺失与真菌生长的减少无关，表明这种细胞壁相关蛋白在A.烟熏。
In the filamentous fungus Aspergillus fumigatus, the vast majority of the cell-wall-associated proteins are secreted proteins that are in transit in the cell wall. These proteins can be solubilized by detergents and reducing agents. Incubation of a SDS/beta-mercaptoethanol-treated cell-wall extract with various recombinant enzymes that hydrolyse cell-wall polysaccharides resulted in the release of a unique protein in minute amounts only after incubation of the cell wall in the presence of 1,3-beta-glucanase. Sequence analysis and biochemical studies showed that this glycoprotein, with an apparent molecular mass of 80 kDa, was an acid phosphatase (PhoAp) that was active on both phosphate monoesters and phosphate diesters. PhoAp is a glycosylphosphatidylinositol-anchored protein that was recovered in the culture filtrate and cell-wall fraction of A. fumigatus after cleavage of its anchor. It is also a phosphate-repressible acid phosphatase. The absence of PhoAp from a phosphate-rich medium was not associated with a reduction in fungal growth, indicating that this cell-wall-associated protein does not play a role in the morphogenesis of A. fumigatus.