| 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 |
| Journal | FEBS Lett |
| Volume | 580 |
| Issue | 2 |
| Pagination | 603-6 |
| Date Published | 2006 Jan 23 |
| ISSN | 0014-5793 |
| Keywords | Acyltransferases, Animals, Disulfides, Gene Targeting, Humans, Membrane Glycoproteins, Multiprotein Complexes, Mutation, Protein Subunits, Protozoan Proteins, Trypanosoma brucei brucei |
| 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. |
| DOI | 10.1016/j.febslet.2005.12.075 |
| Alternate Journal | FEBS Lett. |
| PubMed ID | 16405969 |
Department of Microbiology