Linked Life Data

8369313

Source:http://linkedlifedata.com/resource/pubmed/id/8369313

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
36
pubmed:dateCreated
1993-10-14
pubmed:abstractText
In N-linked core glycosylation, the oligosaccharide Glc3Man9GlcNAc2 is transferred to the tripeptide sequon Asn-X-Ser/Thr. However, this process must be regulated by additional protein signals, since many sequons are either poorly glycosylated or not glycosylated at all. Since N-linked glycosylation can influence protein structure and function, understanding these signals is essential for the design and expression of recombinant glycoproteins. Core glycosylation usually occurs cotranslationally in the rough endoplasmic reticulum (RER) during translocation of nascent proteins. Since only regions of a protein immediately near to a sequon or N-terminal to it are thought to be in the RER when core glycosylation occurs, most models predict that regions C-terminal to the sequon do not influence this process. We tested whether regions C-terminal to a sequon can influence its core glycosylation. Full-length (505 amino acid) rabies virus glycoprotein (RGP) mutants, each containing only one of the three sequons normally present in RGP, were used for these studies. Using a cell-free system, the core glycosylation efficiency at each sequon was determined. Termination codons were then introduced into these mutants at defined sites to produce C-terminal truncations, and the effect of each of these truncations on the core glycosylation efficiency at each sequon was assessed. While deletion of the C-terminal transmembrane and cytoplasmic domains did not affect core glycosylation, more extensive C-terminal deletions did result in altered core glycosylation in a site-specific fashion. Specifically, C-terminal truncations resulting in proteins containing 386 or 344 amino acids decreased the efficiency of core glycosylation at Asn319. This demonstrates that core glycosylation efficiency can be influenced by the presence or absence of regions in a protein more than 68 amino acids C-terminal to a specific glycosylation site.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
14
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
9465-72
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Efficiency of N-linked core glycosylation at asparagine-319 of rabies virus glycoprotein is altered by deletions C-terminal to the glycosylation sequon.
pubmed:affiliation
University of Pennsylvania School of Medicine, Philadelphia.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't