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Biotechnol Appl Biochem

Title:		alpha-Factor pro-peptide N-linked oligosaccharides facilitate secretion of the insulin precursor in Saccharomyces cerevisiae
Author(s):		Kjeldsen T; Andersen AS; Hach M; Diers I; Nikolajsen J; Markussen J;
Address:
Journal Title:		Biotechnol Appl Biochem
Year:		1998
Volume:		27
Issue:		2
Page Number:		109 - 115
DOI:		10.1111/j.1470-8744.1998.tb01382.x
ISSN/ISBN:		0885-4513 (Print) 0885-4513 (Linking)
Abstract:		"To evaluate the possible relationship between N-linked glycosylation of the Saccharomyces cerevisiae alpha-factor pro-peptide and transport of the alpha-factor pro-peptide/insulin precursor fusion protein through the Saccharomyces cerevisiae secretory pathway, we analysed secretion of insulin precursor facilitated by alpha-factor pro-peptides with one or more of the three N-linked glycosylation sites removed. Mutation of the three alpha-factor pro-peptide N-linked glycosylation sites drastically decreased insulin precursor secretion. The three alpha-factor pro-peptide N-linked glycosylation sites differ in their ability to facilitate secretion of the insulin precursor. The two alpha-factor pro-peptide N-linked glycosylation sites localized closest to the insulin precursor contributed significantly to secretion, whereas the most N-terminally linked glycosylation site did not appear to facilitate secretion. Only correctly folded insulin precursor was found in the culture supernatant, regardless of the pro-peptide used for secretion, indicating that alpha-factor pro-peptide N-linked oligosaccharide chains are not necessary for correct folding of the insulin precursor. Thus, N-linked glycosylation facilitates intracellular transport of the alpha-factor propeptide/insulin precursor fusion protein through the Saccharomyces cerevisiae secretory pathway and secretion of the insulin precursor. N-linked glycosylation per se is not sufficient to facilitate secretion of the insulin precursor; the position of the N-linked oligosaccharide chain on the alpha-factor pro-peptide is important for facilitating efficient secretion"
Keywords:		"Binding Sites Chromatography, High Pressure Liquid/methods Electrophoresis, Gel, Pulsed-Field/methods Glycosylation Insulin/chemistry/genetics/*metabolism Insulin Secretion Mass Spectrometry Mating Factor Mutation Oligosaccharides/*metabolism Peptides/*ge;"
Notes:		"MedlineKjeldsen, T Andersen, A S Hach, M Diers, I Nikolajsen, J Markussen, J eng 1998/05/07 Biotechnol Appl Biochem. 1998 Apr; 27(2):109-15. doi: 10.1111/j.1470-8744.1998.tb01382.x"