Linked Life Data

2507249

Source:http://linkedlifedata.com/resource/pubmed/id/2507249

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-11-2
pubmed:abstractText
We have described a new form of protein glycosylation in which N-acetylglucosamine is glycosidically linked to the hydroxyl of serine or threonine (O-GlcNAc). Unlike most other forms of protein glycosylation, O-GlcNAc is predominantly localized in the nuclear and cytoplasmic compartments of cells, where it occurs on important nuclear pore glycoproteins, well-characterized cytoskeletal proteins, as well as on many chromatin proteins, including factors that regulate gene transcription. Gas-phase protein sequencing of three O-GlcNAc-modified proteins has identified a common structural feature at sites of O-GlcNAc addition. An assay for UDP-GlcNAc:polypeptide O-GlcNAc transferase has been developed. The enzyme appears to be membrane-associated, its active site is cytoplasmic, and it has an absolute requirement for Mn2+. We are now purifying this glycosyltransferase, characterizing its substrate specificity, and determining the extent of elongation of attached saccharide moieties. The functions of O-GlcNAc remain largely unknown, but it may be important in blocking phosphorylation sites, it may be required for the assembly of specific multiprotein complexes, it might serve as a nuclear transport signal, or it may be directly involved in the active transport of macromolecules across nuclear pores.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-5208
pubmed:author
pubmed:issnType
Print
pubmed:volume
145
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
102-12, discussion 112-8
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Nucleoplasmic and cytoplasmic glycoproteins.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't