Synthesis of a GPI anchor module suitable for protein post-translational modification.
Eukaryotic cell surface proteins are often modified by a glycosylphosphatidylinositol (GPI) anchor. More than 200 of these post-translationally altered proteins are presently known, a prominent example being the prion protein (PrP). Although the significance of the GPI anchor is well recognized, efforts to study its function are hampered due to its complex chemical nature, which combines hydrophilic glycosyl chains with hydrophobic lipid moieties. Here we describe a general method for the synthesis of a GPI-anchored peptide containing an N-terminal Cys. This module can be employed for the production of proteins containing a natural GPI anchor using expressed protein ligation.
Schumacher
Miria C
MC
Max-Planck Institute of Molecular Physiology, Otto-Hahn-Strasse 11, Dortmund 44227, Germany.
Resenberger
Ulrike
U
Seidel
Ralf P
RP
Becker
Christian F W
CF
Winklhofer
Konstanze F
KF
Oesterhelt
Dieter
D
Tatzelt
Jörg
J
Engelhard
Martin
M
D017261:Glycosylphosphatidylinositols / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics; D006801:Humans; D010455:Peptides / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics; D011328:Prions / Q000096:biosynthesis / Q000138:chemical synthesis* / Q000737:chemistry / Q000235:genetics; D011499:Protein Processing, Post-Translational; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
D017261:Glycosylphosphatidylinositols; D010455:Peptides; D011328:Prions