酵母Gaa1p是将完整的糖基磷脂酰肌醇（GPI）锚连接到蛋白质上所必需的。
Yeast Gaa1p is required for attachment of a completed GPI anchor onto proteins.
作者信息
Hamburger D, Egerton M, Riezman H
机构信息
Biozentrum of the University of Basel, Switzerland.
出版信息
J Cell Biol. 1995 May;129(3):629-39. doi: 10.1083/jcb.129.3.629.
Abstract
Anchoring of proteins to membranes by glycosylphosphatidylinositols (GPIs) is ubiquitous among all eukaryotes and heavily used by parasitic protozoa. GPI is synthesized and transferred en bloc to form GPI-anchored proteins. The key enzyme in this process is a putative GPI:protein transamidase that would cleave a peptide bond near the COOH terminus of the protein and attach the GPI by an amide linkage. We have identified a gene, GAA1, encoding an essential ER protein required for GPI anchoring. gaal mutant cells synthesize the complete GPI anchor precursor at nonpermissive temperatures, but do not attach it to proteins. Overexpression of GAA1 improves the ability of cells to attach anchors to a GPI-anchored protein with a mutant anchor attachment site. Therefore, Gaa1p is required for a terminal step of GPI anchor attachment and could be part of the putative GPI:protein transamidase.
摘要
糖基磷脂酰肌醇（GPI）将蛋白质锚定在膜上的现象在所有真核生物中普遍存在，并且被寄生原生动物大量使用。GPI是整体合成并转移以形成GPI锚定蛋白的。这个过程中的关键酶是一种假定的GPI：蛋白质转酰胺酶，它会切割蛋白质COOH末端附近的肽键，并通过酰胺键连接GPI。我们已经鉴定出一个基因GAA1，它编码GPI锚定所需的一种必需的内质网蛋白。gaal突变细胞在非允许温度下合成完整的GPI锚定前体，但不会将其连接到蛋白质上。GAA1的过表达提高了细胞将锚定物连接到具有突变锚定连接位点的GPI锚定蛋白上的能力。因此，Gaa1p是GPI锚定连接的终端步骤所必需的，并且可能是假定的GPI：蛋白质转酰胺酶的一部分。
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Early lipid intermediates in glycosyl-phosphatidylinositol anchor assembly are synthesized in the ER and located in the cytoplasmic leaflet of the ER membrane bilayer.糖基磷脂酰肌醇锚定组装过程中的早期脂质中间体在内质网中合成，并位于内质网膜双层的胞质小叶中。
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