@article {695, title = {TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.}, journal = {FEBS Lett}, volume = {580}, year = {2006}, month = {2006 Jan 23}, pages = {603-6}, abstract = {Glycosylphosphatidylinositol (GPI) is widely used by eukaryotic cell surface proteins for membrane attachment. De novo synthesized GPI precursors are attached to proteins post-translationally by the enzyme complex, GPI transamidase. TbGPI16, a component of the trypanosome transamidase, shares similarity with human PIG-T. Here, we show that TbGPI16 is the orthologue of PIG-T and an essential component of GPI transamidase by creating a TbGPI16 knockout. TbGPI16 forms a disulfide-linked complex with TbGPI8. A cysteine to serine mutant of TbGPI16 was unable to fully restore the surface expression of GPI-anchored proteins upon transfection into the knockout cells, indicating that its disulfide linkage with TbGPI8 is important for the full transamidase activity.}, keywords = {Acyltransferases, Animals, Disulfides, Gene Targeting, Humans, Membrane Glycoproteins, Multiprotein Complexes, Mutation, Protein Subunits, Protozoan Proteins, Trypanosoma brucei brucei}, issn = {0014-5793}, doi = {10.1016/j.febslet.2005.12.075}, author = {Hong, Yeonchul and Nagamune, Kisaburo and Ohishi, Kazuhito and Morita, Yasu S and Ashida, Hisashi and Maeda, Yusuke and Kinoshita, Taroh} }