alpha-Amylase biosynthesis: evidence for temporal sequence of NH2-terminal peptide cleavage and protein glycosylation.
During the biosynthesis of secretory proteins, an NH2-terminal peptide, referred to as a signal peptide, is cotranslationally cleaved off after the protein enters the cisternal space of the endoplasmic reticulum. It also has been reported that the core glycosylation reaction of some secretory and viral membrane glycoproteins occurs as a cotranslational event. However, despite a huge amount of work, no decisive answer has been given as to the temporal sequence of proteolytic cleavage of the signal peptide and glycosylation on the polysomes for any secretory or membrane glycoprotein. We show here that proteolytically processed and already glycosylated chains of rice seed alpha-amylase exist on the polysomes; furthermore, our results provide direct evidence that glycosylation is preceded by proteolytic processing during the biosynthesis of the alpha-amylase molecule.
D000681:Amylases / Q000096:biosynthesis*; D006023:Glycoproteins / Q000096:biosynthesis*; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism; D010944:Plants; D011132:Polyribosomes / Q000378:metabolism; D014176:Protein Biosynthesis; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals; D013997:Time Factors; D000516:alpha-Amylases / Q000096:biosynthesis*
D006023:Glycoproteins; D010455:Peptides; D021382:Protein Sorting Signals; D000681:Amylases; D000516:alpha-Amylases