TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei
TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei
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DOI：
10.1016/j.febslet.2005.12.075
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发表时间：
2006-01-23
期刊：
影响因子：
3.5
通讯作者：
Kinoshita, T
中科院分区：
文献类型：
--
作者：
Hong, YC;Nagamune, K;Kinoshita, T
糖基磷脂酰肌醇（GPI）被真核细胞表面蛋白广泛用于膜附着。从头合成的GPI前体通过酶复合物GPI转酰胺酶在转录后连接到蛋白质上。TbGPI 16是锥虫转酰胺酶的一种组分，与人PIG-T具有相似性。在这里，我们表明，TbGPI 16是直向同源的PIG-T和GPI转酰胺酶的一个重要组成部分，通过创建一个TbGPI 16敲除。TbGPI 16与TbGP 18形成二硫键连接的复合物。TbGPI 16的半胱氨酸到丝氨酸突变体在转染到敲除细胞中后不能完全恢复GPI锚定蛋白的表面表达，表明其与TbGP 18的二硫键对于完整的转酰胺酶活性是重要的。(c)2005年欧洲生物化学学会联合会。Elsevier B. V.出版，保留所有权利。
Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins posttranstationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGP18. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGP18 is important for the full transamidase activity. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.