Evidence map›Paper›PMID 27601472›Full record

ArticleThe Journal of biological chemistry2016

O-GlcNAcase Is an RNA Polymerase II Elongation Factor Coupled to Pausing Factors SPT5 and TIF1β.

Melissa Resto, Bong-Hyun Kim, Alfonso G Fernandez, Brian J Abraham, Keji Zhao, Brian A Lewis

Erratum issuedOpen access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

24 citing papers in PubMed, 42 citations in OpenAlex.

  1. Dynamic Supercoiling Sponsors Transcription Amplification by MYC.bioRxiv : the preprint server for biology · 2026
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  3. Review
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  5. HumanResearch square · 2025
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  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Role ofPhysiological reviews · 2021
    Review
  17. Article
  18. Article
  19. Catalytic deficiency of O-GlcNAc transferase leads to X-linked intellectual disability.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. Nutrient regulation of signaling and transcription.The Journal of biological chemistry · 2019
    Review
4 · The record

Corrections and comments

  • Erratum issued
    2017
5 · Who and what money

Authors and funding

6 authors at 3 institutions in 1 country.

Melissa RestoFrom the Transcriptional Regulation and Biochemistry Unit, Metabolism Branch, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 30893.
Bong-Hyun KimFrederick National Laboratory for Cancer Research, Leidos Biomedical Research, Inc., Frederick, Maryland 21702.
Alfonso G FernandezFrom the Transcriptional Regulation and Biochemistry Unit, Metabolism Branch, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 30893.
Brian J AbrahamBioinformatics Program, Boston University, Boston, Massachusetts 02215, and.
Keji ZhaoLaboratory of Epigenome Biology, NHLBI, National Institutes of Health, Bethesda, Maryland 20892.
Brian A LewisFrom the Transcriptional Regulation and Biochemistry Unit, Metabolism Branch, Center for Cancer Research, NCI, National Institutes of Health, Bethesda, Maryland 30893, phdbiochemist@gmail.com.
National Institutes of Health · USCenter for Cancer Research · USFrederick National Laboratory for Cancer Research · US

Funding

Genome-wide mapping of histone modificationsZIAHL005801 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI ZHAO, KEJI · 2009 to 2025
$24.0M
6 · The paper itself

Abstract

We describe here the identification and functional characterization of the enzyme O-GlcNAcase (OGA) as an RNA polymerase II elongation factor. Using in vitro transcription elongation assays, we show that OGA activity is required for elongation in a crude nuclear extract system, whereas in a purified system devoid of OGA the addition of rOGA inhibited elongation. Furthermore, OGA is physically associated with the known RNA polymerase II (pol II) pausing/elongation factors SPT5 and TRIM28-KAP1-TIF1β, and a purified OGA-SPT5-TIF1β complex has elongation properties. Lastly, ChIP-seq experiments show that OGA maps to the transcriptional start site/5' ends of genes, showing considerable overlap with RNA pol II, SPT5, TRIM28-KAP1-TIF1β, and O-GlcNAc itself. These data all point to OGA as a component of the RNA pol II elongation machinery regulating elongation genome-wide. Our results add a novel and unexpected dimension to the regulation of elongation by the insertion of O-GlcNAc cycling into the pol II elongation regulatory dynamics.

Indexed as

Antigens, NeoplasmHistone AcetyltransferasesHumansHyaluronoglucosaminidaseNuclear ProteinsRepressor ProteinsRNA Polymerase IITranscriptional Elongation FactorsTranscription Elongation, GeneticTripartite Motif-Containing Protein 28Antigens, NeoplasmHistone AcetyltransferasesHyaluronoglucosaminidaseNuclear ProteinsOGA protein, humanRepressor ProteinsRNA Polymerase IISUPT5H protein, humanTranscriptional Elongation FactorsTRIM28 protein, humanTripartite Motif-Containing Protein 28metabolismO-GlcNAcylationRNA polymerase IItranscriptiontranscription elongation factor

Identifiers

PMID27601472
PMCPMC5077205
OpenAlexW2507874699

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.