Abstract
We demonstrate that the signal peptides of prepro-alpha-factor and preinvertase must be cleaved before Asn-X-Ser/Thr acceptor tripeptides located near the signal peptides of these precursors can be efficiently glycosylated within the endoplasmic reticulum of the yeast Saccharomyces cerevisiae. The data support a model whereby the interaction of a signal peptide with the membrane prevents an acceptor tripeptide juxtaposed to the signal peptide from accessing the oligosaccharyltransferase active site until the signal peptide is cleaved.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Amino Acid Sequence
-
Endoplasmic Reticulum / enzymology*
-
Enzyme Precursors / metabolism
-
Fungal Proteins / genetics
-
Fungal Proteins / metabolism
-
Glycoside Hydrolases / metabolism
-
Glycosylation
-
Hexosyltransferases*
-
Membrane Proteins*
-
Models, Biological
-
Molecular Sequence Data
-
Mutation
-
Peptide Hydrolases
-
Protein Precursors / genetics
-
Protein Precursors / metabolism*
-
Protein Processing, Post-Translational*
-
Saccharomyces cerevisiae
-
Saccharomyces cerevisiae Proteins*
-
Serine Endopeptidases / metabolism*
-
Transferases / metabolism*
-
beta-Fructofuranosidase*
Substances
-
Enzyme Precursors
-
Fungal Proteins
-
MF(ALPHA)1 protein, S cerevisiae
-
Membrane Proteins
-
Protein Precursors
-
Saccharomyces cerevisiae Proteins
-
Transferases
-
Hexosyltransferases
-
dolichyl-diphosphooligosaccharide - protein glycotransferase
-
Glycoside Hydrolases
-
preinvertase
-
beta-Fructofuranosidase
-
Peptide Hydrolases
-
SEC11 protein, S cerevisiae
-
Serine Endopeptidases
-
type I signal peptidase