Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
12
|
| pubmed:dateCreated |
1990-5-24
|
| pubmed:abstractText |
The addition of O-linked N-acetylglucosamine (GlcNAc) to the major nuclear pore complex glycoprotein p62 was examined. Expression of the rat p62 cDNA in transfected monkey cells was detected using a rat p62-specific antipeptide antiserum and two previously described nuclear pore-specific monoclonal antibodies which require O-linked GlcNAc for binding. Although the p62 cDNA was predicted to encode a 54-kDa polypeptide, the product expressed in monkey cells migrated on sodium dodecyl sulfate-polyacrylamide gel electrophoresis as two species of 62 and 59-kDa. Cell-free translation of the p62 in vitro transcript yielded a 59-kDa polypeptide using wheat germ extract and a 62-kDa product using a commercially available rabbit reticulocyte lysate. Several lines of evidence indicated that the 62-kDa rabbit reticulocyte lysate translation product was modified by O-linked N-acetylglucosamine; the protein bound specifically to a wheat germ agglutinin affinity column and was converted to 59 kDa when treated with jack bean beta-acetylglucosaminidase. The 59-kDa unglycosylated wheat germ translation product was converted to the 62-kDa glycosylated form upon incubation with reticulocyte lysate demonstrating that O-linked GlcNAc can be added to p62 post-translationally.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Acetylglucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/Glucosamine,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/nuclear pore protein p62
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
25
|
| pubmed:volume |
265
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
6868-73
|
| pubmed:dateRevised |
2010-11-18
|
| pubmed:meshHeading |
pubmed-meshheading:2182631-Acetylglucosamine,
pubmed-meshheading:2182631-Amino Acid Sequence,
pubmed-meshheading:2182631-Animals,
pubmed-meshheading:2182631-Antibodies, Monoclonal,
pubmed-meshheading:2182631-Cell Line,
pubmed-meshheading:2182631-Chromatography, Affinity,
pubmed-meshheading:2182631-DNA,
pubmed-meshheading:2182631-Fluorescent Antibody Technique,
pubmed-meshheading:2182631-Glucosamine,
pubmed-meshheading:2182631-Glycosylation,
pubmed-meshheading:2182631-Membrane Glycoproteins,
pubmed-meshheading:2182631-Membrane Proteins,
pubmed-meshheading:2182631-Molecular Sequence Data,
pubmed-meshheading:2182631-Molecular Weight,
pubmed-meshheading:2182631-Nuclear Pore Complex Proteins,
pubmed-meshheading:2182631-Protein Biosynthesis,
pubmed-meshheading:2182631-Protein Processing, Post-Translational,
pubmed-meshheading:2182631-Rats,
pubmed-meshheading:2182631-Reticulocytes,
pubmed-meshheading:2182631-Transfection
|
| pubmed:year |
1990
|
| pubmed:articleTitle |
Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro.
|
| pubmed:affiliation |
Laboratory of Biochemistry and Metabolism, National Institute of Diabetes, Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892.
|
| pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|