Yoda K, Ko J H, Nagamatsu T, Lin Y, Kaibara C, Kawada T, Tomishige N, Hashimoto H, Noda Y, Yamasaki M
Department of Biotechnology, University of Tokyo, Japan.
Biosci Biotechnol Biochem. 2000 Jan;64(1):142-8. doi: 10.1271/bbb.64.142.
A novel Kluyveromyces marxianus gene that encodes an acid phosphatase, Pho610, was cloned in Saccharomyces cerevisiae. The deduced amino acid sequence was distinct from S. cerevisiae phosphatases but similar to some fungal enzymes. A peculiar feature of the sequence is that it has hydrophobic stretches both at the N- and C-termini, which is a characteristic of the precursors of glycosylphosphatidylinositol(GPI)-anchored proteins. When the gene was expressed in S. cerevisiae, the active enzyme was recovered in the periplasmic fraction by glucanase digestion. The Pho610 polypeptide was highly glycosylated and a significant portion was covalently linked to the cell-wall glucan. The enzyme was secreted when the C-terminal region was truncated to remove the GPI signal. Therefore, Pho610 is a novel cell-wall protein having an enzyme activity.
一个编码酸性磷酸酶Pho610的新型马克思克鲁维酵母基因在酿酒酵母中被克隆出来。推导的氨基酸序列与酿酒酵母的磷酸酶不同，但与一些真菌酶相似。该序列的一个独特特征是，它在N端和C端都有疏水片段，这是糖基磷脂酰肌醇（GPI）锚定蛋白前体的一个特征。当该基因在酿酒酵母中表达时，通过葡聚糖酶消化，活性酶在周质部分被回收。Pho610多肽高度糖基化，并且很大一部分与细胞壁葡聚糖共价连接。当C端区域被截短以去除GPI信号时，该酶被分泌出来。因此，Pho610是一种具有酶活性的新型细胞壁蛋白。
