Title : Glycosylation of nuclear pore protein p62. Reticulocyte lysate catalyzes O-linked N-acetylglucosamine addition in vitro.

Pub. Date : 1990 Apr 25

PMID : 2182631






5 Functional Relationships(s)
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1 The addition of O-linked N-acetylglucosamine (GlcNAc) to the major nuclear pore complex glycoprotein p62 was examined. 2-acetamido-2-deoxy-4-O-(beta-2-acetamid-2-deoxyglucopyranosyl)glucopyranose KH RNA binding domain containing, signal transduction associated 1 Rattus norvegicus
2 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. o-linked glcnac KH RNA binding domain containing, signal transduction associated 1 Rattus norvegicus
3 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. Sodium Dodecyl Sulfate KH RNA binding domain containing, signal transduction associated 1 Rattus norvegicus
4 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. polyacrylamide KH RNA binding domain containing, signal transduction associated 1 Rattus norvegicus
5 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. o-linked glcnac KH RNA binding domain containing, signal transduction associated 1 Rattus norvegicus