UMMS Affiliation

Department of Biochemistry and Molecular Pharmacology

Date

4-4-2007

Document Type

Article

Subjects

Animals; Binding Sites; Cryptococcus neoformans; Dolichol; Entamoeba histolytica; Fungal Proteins; Hexosyltransferases; Kinetics; Mannose; Membrane Proteins; Oligosaccharides; Protozoan Proteins; Saccharomyces cerevisiae; Substrate Specificity; Trichomonas vaginalis; Trypanosoma cruzi

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

The dolichol-linked oligosaccharide Glc3Man9GlcNAc2-PP-Dol is the in vivo donor substrate synthesized by most eukaryotes for asparagine-linked glycosylation. However, many protist organisms assemble dolichol-linked oligosaccharides that lack glucose residues. We have compared donor substrate utilization by the oligosaccharyltransferase (OST) from Trypanosoma cruzi, Entamoeba histolytica, Trichomonas vaginalis, Cryptococcus neoformans, and Saccharomyces cerevisiae using structurally homogeneous dolichol-linked oligosaccharides as well as a heterogeneous dolichol-linked oligosaccharide library. Our results demonstrate that the OST from diverse organisms utilizes the in vivo oligo saccharide donor in preference to certain larger and/or smaller oligosaccharide donors. Steady-state enzyme kinetic experiments reveal that the binding affinity of the tripeptide acceptor for the protist OST complex is influenced by the structure of the oligosaccharide donor. This rudimentary donor substrate selection mechanism has been refined in fungi and vertebrate organisms by the addition of a second, regulatory dolichol-linked oligosaccharide binding site, the presence of which correlates with acquisition of the SWP1/ribophorin II subunit of the OST complex.

Rights and Permissions

Citation: J Cell Biol. 2007 Apr 9;177(1):29-37. Epub 2007 Apr 2. Link to article on publisher's site

DOI of Published Version

10.1083/jcb.200611079

Related Resources

Link to Article in PubMed

Journal Title

The Journal of cell biology glycotransferase)

PubMed ID

17403929

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