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Volume 272, Number 25, Issue of June 20, 1997 pp. 15834-15840
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Expression Cloning of PIG-L, a Candidate N-Acetylglucosaminyl-phosphatidylinositol Deacetylase

(Received for publication, October 30, 1996, and in revised form, March 5, 1997)

Nobuo Nakamura , Norimitsu Inoue , Reika Watanabe , Minoru Takahashi , Junji Takeda , Victoria L. Stevens and Taroh Kinoshita

From the Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka University, Osaka 565, Japan and the  Division of Cancer Biology, Department of Radiation Oncology and Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30335

Many eukaryotic cell surface proteins are bound to the cell membrane by a glycosylphosphatidylinositol (GPI) anchor. Several genes involved in GPI anchor biosynthesis have been cloned using complementation of mutant mammalian cell lines and yeasts that are defective in its biosynthesis pathway. However, the gene involved in the second step of this pathway, in which N-acetylglucosaminyl-phosphatidylinositol (GlcNAc-PI) is N-deacetylated to form glucosaminyl (GlcN)-PI, has not been cloned. In this study, we established a GPI anchor-deficient mutant of Chinese hamster ovary (CHO) cells defective in the second step. Complementation analysis with the known GPI anchor mutant cells demonstrated that it belonged to the same complementation group as the CHO cell mutant G9PLAP.85. Using the new mutant, we cloned a rat gene termed PIG-L (for phosphatidylinositol glycan class L) that is involved in this step. PIG-L encodes a 252-amino acid, endoplasmic reticulum membrane protein, most of which is in the cytoplasmic side. This orientation of PIG-L protein is consistent with the notion that the second step of GPI anchor biosynthesis occurs on the cytoplasmic side of the endoplasmic reticulum.

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