Linked Life Data

8317108

Source:http://linkedlifedata.com/resource/pubmed/id/8317108

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-7-23
pubmed:abstractText
We have previously shown that the early region E3 of adenovirus type 2 encodes a 6700 MW (6.7K) protein. This protein is immunoprecipitated from infected cells as two series of bands, a doublet at 7-8K and a doublet or triplet at 15-16K. The predicted amino acid sequence of the 6.7K indicates that there are three potential Asn-linked glycosylation sites near the N-terminus of the protein. Studies done using tunicamycin, endoglycosaminidase H (endo H), and endo F demonstrate that 6.7K has exclusively high mannose oligosaccharides and that only one of the three potential glycosylation sites of 6.7K is glycosylated. [3H]-Mannose labeling confirmed that the upper species of 6.7K were glycosylated. Since the oligosaccharides are not processed from high mannose to the complex type, this implies that the 6.7K protein is retained in the endoplasmic reticulum (ER). This was confirmed with immunofluorescence. Based on the predicted amino acid sequence, 6.7K does not have a classical N-terminus signal sequence, but it does have a 22 amino acid hydrophobic domain, located at amino acids 15-36, that could function as a signal-anchor domain. We demonstrate that the 6.7K protein is an integral membrane ER protein. Considering that all of the potential Asn-glycosylation sites are near the N-terminus of 6.7K, it must be oriented in the membrane with its N-terminus in the lumen of the ER and its C-terminus in the cytoplasm. Pulse-chase studies performed to examine the temporal appearance of the different 6.7K moieties suggests that this protein may translocate into the ER membrane post-translationally, or may be glycosylated post-translationally.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6-15
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The E3-6.7K protein of adenovirus is an Asn-linked integral membrane glycoprotein localized in the endoplasmic reticulum.
pubmed:affiliation
Department of Molecular Microbiology and Immunology, St. Louis University School of Medicine, Missouri 63104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.