A MUCOR PUSILLUS MUTANT DEFECTIVE IN ASPARAGINE-LINKED GLYCOSYLATION

Citation
K. Murakami et al., A MUCOR PUSILLUS MUTANT DEFECTIVE IN ASPARAGINE-LINKED GLYCOSYLATION, Journal of bacteriology, 176(9), 1994, pp. 2635-2639
Citations number
35
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Microbiology
Journal title
ISSN journal
0021-9193
Volume
176
Issue
9
Year of publication
1994
Pages
2635 - 2639
Database
ISI
SICI code
0021-9193(1994)176:9<2635:AMPMDI>2.0.ZU;2-4
Abstract
A Mucor pusillus mutant defective in asparagine-linked glycosylation w as found in our stock cultures. This mutant, designated 1116, secreted aspartic proteinase (MPP) in a less-glycosylated form than that secre ted by the wild-type strain. Analysis of enzyme susceptibility, lectin binding, and carbohydrate composition indicated that this mutant secr eted three glycoforms of MPPs, one of which contained no carbohydrate; the other two had truncated asparagine-linked oligosaccharide chains such as Man(0 similar to 1)GlcNAc(2). Further analysis using oligosacc haride processing inhibitors, such as castanospermine, 1-deoxynojirimy cin and N-methyldeoxynojirimycin, suggested that MPPs in the mutant we re glycosylated through a transfer of the truncated lipid-linked oligo saccharides, Man(0 similar to 1)GlcNAc(2), to the MPP protein but not through an aberrant processing. In addition, genetic studies with forc ed primary heterokaryons indicated that the mutation in strain 1116 wa s recessive.