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TbGPI16 is an essential component of GPI transamidase in Trypanosoma brucei
Author(s) -
Hong Yeonchul,
Nagamune Kisaburo,
Ohishi Kazuhito,
Morita Yasu S.,
Ashida Hisashi,
Maeda Yusuke,
Kinoshita Taroh
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.12.075
Subject(s) - trypanosoma brucei , serine , mutant , cysteine , transfection , microbiology and biotechnology , biochemistry , disulfide bond , biology , disulfide linkage , enzyme , chemistry , gene
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.