Title

Topography of glycosylation in yeast: characterization of GDPmannose transport and lumenal guanosine diphosphatase activities in Golgi-like vesicles

UMMS Affiliation

Department of Biochemistry

Publication Date

9-1-1989

Document Type

Article

Subjects

Biological Transport; Cytoplasm; Glycosylation; Golgi Apparatus; Guanosine Diphosphate Mannose; Hydrolysis; Kinetics; Models, Biological; Nucleoside Diphosphate Sugars; Pyrophosphatases; Ribonucleotides; Saccharomyces cerevisiae; Subcellular Fractions

Disciplines

Life Sciences | Medicine and Health Sciences

Abstract

"Outer-chain" addition of mannose residues to yeast glycoproteins occurs in the Golgi compartment of the cell. Essential steps in this process are thought to include transport of GDPmannose from the cytoplasm into the lumen of Golgi vesicles, transfer of mannose to glycoprotein acceptors, hydrolysis of the resulting GDP to GMP, and return of GMP and inorganic phosphate to the cytoplasm. We report detection and characterization of a GDPmannose transport activity and a GDPase by yeast vesicles. The active transport of GDPmannose as well as the GDPase and another presumed Golgi enzyme, alpha 1,2-mannosyltransferase, are concentrated in a subcellular fraction that can be partially separated, by velocity sucrose gradient centrifugation, from a fraction enriched in an endoplasmic reticulum marker enzyme.

Rights and Permissions

Citation: Proc Natl Acad Sci U S A. 1989 Sep;86(18):6935-9.

Related Resources

Link to Article in PubMed

Journal/Book/Conference Title

Proceedings of the National Academy of Sciences of the United States of America

PubMed ID

2476806