|Title||TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei.|
|Publication Type||Journal Article|
|Year of Publication||2006|
|Authors||Hong Y, Nagamune K, Ohishi K, Morita YS, Ashida H, Maeda Y, Kinoshita T|
|Date Published||2006 Jan 23|
|Keywords||Acyltransferases, Animals, Disulfides, Gene Targeting, Humans, Membrane Glycoproteins, Multiprotein Complexes, Mutation, Protein Subunits, Protozoan Proteins, Trypanosoma brucei brucei|
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.
|Alternate Journal||FEBS Lett.|