Linked Life Data

8486697

Source:http://linkedlifedata.com/resource/pubmed/id/8486697

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
14
pubmed:dateCreated
1993-6-8
pubmed:abstractText
The largest subunit of mammalian RNA polymerase II (RNAP II) contains at its carboxyl terminus an unusual domain consisting of 52 tandem repeats of the consensus sequence Tyr-Ser-Pro-Thr-Ser-Pro-Ser. This domain, designated the COOH-terminal domain (CTD), is essential for viability and is extensively phosphorylated during the transition from preinitiation complex assembly to elongation (1). Indeed, phosphorylation of the CTD may play an important regulatory role in this transition. We show here that the CTD is also modified by a novel form of protein glycosylation, O-GlcNAc. This modification has been found on numerous transcription factors and other nuclear and cytosolic proteins (2). Glycopeptides obtained by proteolytic digestion of the CTD were purified by reverse-phase high performance liquid chromatography and sequenced. Results from such experiments suggest that glycosylation occurs at multiple sites throughout the CTD, similar to the phosphorylation of this domain. The carbohydrate, however, is not detectable on the phosphorylated form of the enzyme. This observation is consistent with the idea that phosphorylation and glycosylation are mutually exclusive modifications. The CTD of RNAP II, therefore, appears to exist in three distinct conformational states: unmodified, phosphorylated, and glycosylated. The differential modification of the CTD may play an important role in the regulated expression of genes transcribed by RNA polymerase II.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
268
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10416-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:8486697-Acetylglucosamine, pubmed-meshheading:8486697-Amino Acid Sequence, pubmed-meshheading:8486697-Animals, pubmed-meshheading:8486697-Blotting, Western, pubmed-meshheading:8486697-Cattle, pubmed-meshheading:8486697-Chromatography, High Pressure Liquid, pubmed-meshheading:8486697-Female, pubmed-meshheading:8486697-Galactosyltransferases, pubmed-meshheading:8486697-Glycopeptides, pubmed-meshheading:8486697-Glycoproteins, pubmed-meshheading:8486697-Glycosylation, pubmed-meshheading:8486697-Macromolecular Substances, pubmed-meshheading:8486697-Mice, pubmed-meshheading:8486697-Milk, pubmed-meshheading:8486697-Molecular Sequence Data, pubmed-meshheading:8486697-Peptide Fragments, pubmed-meshheading:8486697-Pronase, pubmed-meshheading:8486697-RNA Polymerase II, pubmed-meshheading:8486697-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:8486697-Sequence Homology, Amino Acid, pubmed-meshheading:8486697-Thymus Gland, pubmed-meshheading:8486697-Uridine Diphosphate Galactose
pubmed:year
1993
pubmed:articleTitle
RNA polymerase II is a glycoprotein. Modification of the COOH-terminal domain by O-GlcNAc.
pubmed:affiliation
Department of Biological Chemistry, Johns Hopkins School of Medicine, Baltimore, Maryland 21205.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't