Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II

F. I. Comer, Gerald Warren Hart

Research output: Contribution to journalArticle

Abstract

The carboxyl terminal domain of RNA polymerase II has multiple essential roles in transcription initiation, promoter clearance, transcript elongation, and the recruitment of the RNA processing machinery. Specific phosporylation events are associated with the spatial and temporal coordination of these different activities. The CTD is also modified by β-O-linked GlcNAc on a subset of RNA Pol II molecules. Using synthetic CTD substrates, we show here that O-GlcNAc and phosphate modification of the CTD are mutually exclusive at the level of the enzymes responsible for their addition. In addition, we show that O-GlcNAc transferase and CTD kinase have different CTD repeat requirements for enzymatic activity. The Km values of the two enzymes for CTD substrates are in a similar range, indicating that neither enzyme has a distinct kinetic advantage. Thus, the in vivo regulation of O-GlcNAc and phosphate modification of the CTD may involve the differential association of these two enzymes with the CTD at specific stages during the transcription cycle. Furthermore, direct competition between OGT and CTD kinase in vivo could generate multiple functionally distinct isoforms of RNA Pol II. Taken together, these results suggest that O-GlcNAc may give rise to additional functional states of RNA Pol II and may coordinate with phosphorylation to regulate class II gene transcription.

Original languageEnglish (US)
Pages (from-to)7845-7852
Number of pages8
JournalBiochemistry®
Volume40
Issue number26
DOIs
StatePublished - Jul 3 2001

Fingerprint

RNA Polymerase II
Transcription
Phosphates
N-acetylglucosamine kinase
Enzymes
MHC Class II Genes
Phosphorylation
Substrates
Machinery
Elongation
Protein Isoforms
Genes
Association reactions
RNA
Molecules
Kinetics
Processing
carboxy-terminal domain kinase

ASJC Scopus subject areas

  • Biochemistry

Cite this

Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. / Comer, F. I.; Hart, Gerald Warren.

In: Biochemistry®, Vol. 40, No. 26, 03.07.2001, p. 7845-7852.

Research output: Contribution to journalArticle

Comer, F. I. ; Hart, Gerald Warren. / Reciprocity between O-GlcNAc and O-phosphate on the carboxyl terminal domain of RNA polymerase II. In: Biochemistry®. 2001 ; Vol. 40, No. 26. pp. 7845-7852.
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