Ontology highlight
ABSTRACT:
SUBMITTER: Nagamune K
PROVIDER: S-EPMC196864 | biostudies-literature | 2003 Sep
REPOSITORIES: biostudies-literature
Nagamune Kisaburo K Ohishi Kazuhito K Ashida Hisashi H Hong Yeonchul Y Hino Jun J Kangawa Kenji K Inoue Norimitsu N Maeda Yusuke Y Kinoshita Taroh T
Proceedings of the National Academy of Sciences of the United States of America 20030904 19
Glycosylphosphatidylinositol (GPI) anchor is a membrane attachment mechanism for cell surface proteins widely used in eukaryotes. GPIs are added to proteins posttranslationally by a complex enzyme, GPI transamidase. Previous studies have shown that human and Saccharomyces cerevisiae GPI transamidases are similar and consist of five homologous components: GAA1, GPI8, PIG-S, PIG-T, and PIG-U in humans and Gaa1p, Gpi8p, Gpi17p, Gpi16p, and Cdc91p in S. cerevisiae. We report that GPI transamidase of ...[more]