Document Detail


Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding.
MedLine Citation:
PMID:  18343219     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Prion protein (PrP) contains two N-linked glycosylation sites. It is unknown which amino acid substitution contributes most efficiently to the abolishment of N-linked glycosylations. To define the influence of amino acid substitution at the N-linked glycosylation sites on the conversion efficiency of mouse PrP, we tested each of all 19 amino acid substitutions at either one of the N-linked glycosylation sites (codon 180, 182, 196 or 198). The conversion efficiency of the mutagenized PrP was highly dependent on the newly introduced amino acid itself regardless of the absence of N-linked glycosylation in scrapie-infected mouse neuroblastoma cells. The majority of mutant PrP with substitutions at the Asn residues of the N-linked glycosylation sites were conversion-competent, whereas most mutant PrP with substitutions at the Thr residues were conversion-incompetent. These findings emphasize that the Asn residues of the N-linked glycosylation sites are replaceable to abolish N-linked glycosylations without directly affecting the protein function.
Authors:
Shino Ikeda; Atsushi Kobayashi; Tetsuyuki Kitamoto
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2008-03-14
Journal Detail:
Title:  Biochemical and biophysical research communications     Volume:  369     ISSN:  1090-2104     ISO Abbreviation:  Biochem. Biophys. Res. Commun.     Publication Date:  2008 May 
Date Detail:
Created Date:  2008-04-03     Completed Date:  2008-05-14     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0372516     Medline TA:  Biochem Biophys Res Commun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1195-8     Citation Subset:  IM    
Affiliation:
Division of CJD Science and Technology, Department of Prion Research, Tohoku University Graduate School of Medicine, 2-1 Seiryo-machi, Aoba-ku, Sendai 980-8575, Japan.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Substitution
Animals
Asparagine / chemistry*,  genetics
Cell Line
Glycosylation
Mice
Mutation
Prions / chemistry*,  genetics
Protein Folding*
Threonine / chemistry*,  genetics
Chemical
Reg. No./Substance:
0/Prions; 7006-34-0/Asparagine; 72-19-5/Threonine

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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