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Vol. 12, Issue 10, 3295-3306, October 2001
*Institute of Biochemistry, University of Fribourg, Switzerland;
and Gpi8p and Gaa1p are essential components of the GPI transamidase
that adds glycosylphosphatidylinositols (GPIs) to newly synthesized proteins. After solubilization in 1.5% digitonin and separation by
blue native PAGE, Gpi8p is found in 430-650-kDa protein complexes. These complexes can be affinity purified and are shown to consist of
Gaa1p, Gpi8p, and Gpi16p (YHR188c). Gpi16p is an essential N-glycosylated transmembrane glycoprotein. Its bulk resides on the
lumenal side of the ER, and it has a single C-terminal transmembrane domain and a small C-terminal, cytosolic extension with an ER retrieval
motif. Depletion of Gpi16p results in the accumulation of the complete
GPI lipid CP2 and of unprocessed GPI precursor proteins. Gpi8p and
Gpi16p are unstable if either of them is removed by depletion.
Similarly, when Gpi8p is overexpressed, it largely remains outside the
430-650-kDa transamidase complex and is unstable. Overexpression of
Gpi8p cannot compensate for the lack of Gpi16p. Homologues of Gpi16p
are found in all eucaryotes. The transamidase complex is not associated
with the Sec61p complex and oligosaccharyltransferase complex required
for ER insertion and N-glycosylation of GPI proteins, respectively.
When GPI precursor proteins or GPI lipids are depleted, the
transamidase complex remains intact.
Laboratoire de Spectrométrie de Masse
Bio-Organique, UMR CNRS 7509, 67008 Strasbourg Cedex, France
These authors contributed equally to this work.
§
Corresponding author. E-mail:
andreas.conzelmann{at}unifr.ch. Present address: Institute of
Biochemistry, Chemin du Musée 5, CH-1700 Fribourg, Switzerland.
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