| Literature DB >> 16405969 |
Yeonchul Hong1, Kisaburo Nagamune, Kazuhito Ohishi, Yasu S Morita, Hisashi Ashida, Yusuke Maeda, Taroh Kinoshita.
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.Entities:
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Year: 2006 PMID： 16405969 DOI： 10.1016/j.febslet.2005.12.075
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124