ArticleBiochemistry2016
Distributive O-GlcNAcylation on the Highly Repetitive C-Terminal Domain of RNA Polymerase II.
Article in Biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 30 citations in OpenAlex.
- Quantitative modelling of P-TEFb mediated CTD phosphorylation identifies local cooperativity.PLoS computational biology · 2026Article
- Dynamic O-GlcNAcylation and phosphorylation attract and expel proteins from RNA polymerase II to regulate mRNA maturation.Journal of biomedical science · 2025Article
- SETD5 regulates the OGT-catalyzed O-GlcNAcylation of RNA polymerase II, which is involved in the stemness of colorectal cancer cells.Scientific reports · 2023Article
- Tools, tactics and objectives to interrogate cellular roles of O-GlcNAc in disease.Nature chemical biology · 2022Review
- A nexus of lipid andFrontiers in endocrinology · 2022Review
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- Role ofPhysiological reviews · 2021Review
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- A combinatorial view of old and new RNA polymerase II modifications.Transcription · 2020Review
- Processivity in Bacterial Glycosyltransferases.ACS chemical biology · 2020Review
- O-GlcNAc in cancer: An Oncometabolism-fueled vicious cycle.Journal of bioenergetics and biomembranes · 2018Review
- Nutrient-DrivenFrontiers in endocrinology · 2018Article
- The emerging link between O-GlcNAcylation and neurological disorders.Cellular and molecular life sciences : CMLS · 2017Review
- Deciphering the Functions of Protein O-GlcNAcylation with Chemistry.ACS chemical biology · 2017Review
- The pol II CTD: new twists in the tail.Nature structural & molecular biology · 2016Review
- Interplay between Metabolism and Epigenetics: A Nuclear Adaptation to Environmental Changes.Molecular cell · 2016Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
O-GlcNAcylation is a nutrient-responsive glycosylation that plays a pivotal role in transcriptional regulation. Human RNA polymerase II (Pol II) is extensively modified by O-linked N-acetylglucosamine (O-GlcNAc) on its unique C-terminal domain (CTD), which consists of 52 heptad repeats. One approach to understanding the function of glycosylated Pol II is to determine the mechanism of dynamic O-GlcNAcylation on the CTD. Here, we discovered that the Pol II CTD can be extensively O-GlcNAcylated in vitro and in cells. Efficient glycosylation requires a minimum of 20 heptad repeats of the CTD and more than half of the N-terminal domain of O-GlcNAc transferase (OGT). Under conditions of saturated sugar donor, we monitored the attachment of more than 20 residues of O-GlcNAc to the full-length CTD. Surprisingly, glycosylation on the periodic CTD follows a distributive mechanism, resulting in highly heterogeneous glycoforms. Our data suggest that initial O-GlcNAcylation can take place either on the proximal or on the distal region of the CTD, and subsequent glycosylation occurs similarly over the entire CTD with nonuniform distributions. Moreover, removal of O-GlcNAc from glycosylated CTD is also distributive and is independent of O-GlcNAcylation level. Our results suggest that O-GlcNAc cycling enzymes can employ a similar mechanism to react with other protein substrates on multiple sites. Distributive O-GlcNAcylation on Pol II provides another regulatory mechanism of transcription in response to fluctuating cellular conditions.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.