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Vol. 11, Issue 5, 1523-1533, May 2000
and
*Department of Immunoregulation, Research Institute for Microbial
Diseases, Osaka University, Osaka 565-0871, Japan; and
Many eukaryotic cell surface proteins are anchored to the membrane
via glycosylphosphatidylinositol (GPI). The GPI is attached to
proteins that have a GPI attachment signal peptide at the carboxyl terminus. The GPI attachment signal peptide is replaced by a
preassembled GPI in the endoplasmic reticulum by a transamidation
reaction through the formation of a carbonyl intermediate. GPI
transamidase is a key enzyme of this posttranslational modification.
Here we report that Gaa1p and Gpi8p are components of a GPI
transamidase. To determine a role of Gaa1p we disrupted a
GAA1/GPAA1 gene in mouse F9 cells by homologous
recombination. GAA1 knockout cells were defective in the
formation of carbonyl intermediates between precursor proteins and
transamidase as determined by an in vitro GPI-anchoring assay. We also
show that cysteine and histidine residues of Gpi8p, which are conserved
in members of a cysteine protease family, are essential for generation
of a carbonyl intermediate. This result suggests that Gpi8p is a
catalytic component that cleaves the GPI attachment signal peptide.
Moreover, Gaa1p and Gpi8p are associated with each other. Therefore,
Gaa1p and Gpi8p constitute a GPI transamidase and cooperate in
generating a carbonyl intermediate, a prerequisite for GPI attachment.
Biozentrum, University of Basel, Basel CH-4056,
Switzerland
Corresponding author. E-mail address:
tkinoshi{at}biken.osaka-u.ac.jp.
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