NDLI: Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability.

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Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability.

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Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Kosman, Daniel J. Ziegler, Lynn Terzulli, Alaina Sedlak, Erik
Description	Country affiliation: United States Author Affiliation: Ziegler L ( Department of Biochemistry, School of Medicine and Biomedical Sciences, State University of New York, Buffalo, New York 14214-3000, USA.)
Abstract	Glycosylation is essential to the maintenance of protein quality in the vesicular protein trafficking pathway in eukaryotic cells. Using the yeast multicopper oxidase, Fet3p, the hypothesis is tested that core glycosylation suppresses Fet3p nascent chain aggregation during synthesis into the endoplasmic reticulum (ER). Fet3p has 11 crystallographically mapped N-linked core glycan units. Assembly of four of these units is specifically required for localization of Fet3p to the plasma membrane (PM). Fet3 protein lacking any one of these glycan units is found in an intracellular high-molecular mass species resolvable by blue native gel electrophoresis. Individually, the remaining glycan moieties are not required for ER exit; however, serial deletion of these by N â A substitution correlates with these desglycan species failure to exit the ER. Desglycan Fet3 proteins that localize to the PM are wild type in function indicating that the missing carbohydrate is not required for native structure and biologic activity. This native function includes the interaction with the iron permease, Ftr1p, and wild type high-affinity iron uptake activity. The four essential sequons are found within relatively nonpolar regions located in surface recesses and are strongly conserved among fungal Fet3 proteins. The remaining N-linked sites are found in more surface exposed, less nonpolar environments, and their conservation is weak or absent. The data indicate that in Fet3p the N-linked glycan has little effect on the enzyme's molecular activity but is critical to its cellular activity by maximizing the protein's exit from the ER and assembly into a functional iron uptake complex.
ISSN	09618368
e-ISSN	1469896X
DOI	10.1002/pro.457
Journal	Protein Science
Issue Number	9
Volume Number	19
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2010-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Ceruloplasmin Chemistry Metabolism Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Amino Acid Sequence Genetics Glycosylation Models, Molecular Molecular Sequence Data Mutation Protein Folding Protein Stability Protein Transport Structural Homology, Protein Research Support, N.i.h., Extramural Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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