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. 1996 Dec 2;15(23):6575–6583.

Yeast Gpi8p is essential for GPI anchor attachment onto proteins.

M Benghezal 1, A Benachour 1, S Rusconi 1, M Aebi 1, A Conzelmann 1
PMCID: PMC452482  PMID: 8978684

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.

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