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Yeast Gpi8p is essential for GPI anchor attachment onto proteins.
Author(s) -
Benghezal M.,
Benachour A.,
Rusconi S.,
Aebi M.,
Conzelmann A.
Publication year - 1996
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1002/j.1460-2075.1996.tb01048.x
Subject(s) - library science , biology , biochemistry , bioinformatics , computer science
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.