Linked Life Data

3545316

Source:http://linkedlifedata.com/resource/pubmed/id/3545316

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
1987-4-14
pubmed:abstractText
When programmed with yeast prepro-alpha-factor mRNA, the heterologous reticulocyte/dog pancreas translation system synthesizes two pheromone related polypeptides, a cytosolically located primary translation product (pp-alpha-Fcyt, 21 kDa) and a membrane-specific and multiply glycosylated alpha-factor precursor (pp-alpha-F3, 27.5 kDa). Glycosylation of the membrane specific pp-alpha-F3 species is competitively inhibited by synthetic peptides containing the consensus sequence Asn-Xaa-Thr as indicated by a shift of its molecular mass from 27.5 kDa to about 19.5 kDa (pp-alpha-F0), whereas the primary translation product pp-alpha-Fcyt is not affected. Likewise, only the glycosylated pp-alpha-F3 structure is digested by Endo H yielding a polypeptide with a molecular mass between pp-alpha-F0 and pp-alpha-Fcyt. These observations strongly suggest that the primary translation product is proteolytically processed during/on its translocation into the lumen of the microsomal vesicles. We believe that this proteolytic processing is due to the cleavage of a signal sequence from the pp-alpha-Fcyt species, although this interpretation contradicts previous data from other groups. The distinct effect exerted by various glycosidase inhibitors (e.g. 1-deoxynojirimycin, N-methyl-dNM, 1-deoxymannojirimycin) on the electrophoretic mobility of the pp-alpha-F3 polypeptide indicates that its oligosaccharide chains are processed to presumably Man9-GlcNAc2 structures under the in vitro conditions of translation. This oligosaccharide processing is most likely to involve the action of glucosidase I and glucosidase II as follows from the specificity of the glycosidase inhibitors applied and the differences of the molecular mass observed in their presence.(ABSTRACT TRUNCATED AT 250 WORDS)
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0144-8463
pubmed:author
pubmed:issnType
Print
pubmed:volume
6
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
827-34
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
In vitro studies on the subcellular location of glucosidase I and glucosidase II in dog pancreas.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't