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Yeast Gpi8p is essential for GPI anchor attachment onto proteins.


ABSTRACT: Glycosylphosphatidylinositol (GPI) anchors are added onto newly synthesized proteins in the ER. Thereby a putative transamidase removes a C-terminal peptide and attaches the truncated protein to the free amino group of the preformed GPI. The yeast mutant gpi8-1 is deficient in this addition of GPIs to proteins. GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. GPI8 shows significant homology to a novel family of vacuolar plant endopeptidases one of which is supposed to catalyse a transamidation step in the maturation of concanavalin A and acts as a transamidase in vitro. Humans have a gene which is highly homologous to GPI8 and can functionally replace it.

SUBMITTER: Benghezal M 

PROVIDER: S-EPMC452482 | biostudies-other | 1996 Dec

REPOSITORIES: biostudies-other

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Yeast Gpi8p is essential for GPI anchor attachment onto proteins.

Benghezal M M   Benachour A A   Rusconi S S   Aebi M M   Conzelmann A A  

The EMBO journal 19961201 23


Glycosylphosphatidylinositol (GPI) anchors are added onto newly synthesized proteins in the ER. Thereby a putative transamidase removes a C-terminal peptide and attaches the truncated protein to the free amino group of the preformed GPI. The yeast mutant gpi8-1 is deficient in this addition of GPIs to proteins. GPI8 encodes for an essential 47 kDa type I membrane glycoprotein residing on the luminal side of the ER membrane. GPI8 shows significant homology to a novel family of vacuolar plant endo  ...[more]

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