Evidence map›Paper›PMID 32084124›Full record

ArticlePLoS genetics2020

Identification of a novel base J binding protein complex involved in RNA polymerase II transcription termination in trypanosomes.

Rudo Kieft, Yang Zhang, Alexandre P Marand, Jose Dagoberto Moran, Robert Bridger, Lance Wells, Robert J Schmitz, Robert Sabatini

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

23 citing papers in PubMed, 49 citations in OpenAlex.

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  14. Impact of Genetic Diversity and Genome Plasticity ofFrontiers in cellular and infection microbiology · 2022
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

8 authors at 1 institution in 1 country.

Rudo KieftDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0002-6494-1884
Yang ZhangDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.
Alexandre P MarandDepartment of Genetics, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0001-9100-8320
Jose Dagoberto MoranDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0003-0991-4194
Robert BridgerDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0003-2653-8813
Lance WellsDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.
Robert J SchmitzDepartment of Genetics, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0001-7538-6663
Robert SabatiniDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia, United States of America.ORCID 0000-0002-0188-0201
University of Georgia · US

Funding

Regulation of RNA polymerase II transcription in trypanosomatidsR01AI109108 · NIAID · UNIVERSITY OF GEORGIA · PI SABATINI, ROBERT S · 2014 to 2022
$3.7M
NIAID NIH HHS R01 AI109108
6 · The paper itself

Abstract

Base J, β-D-glucosyl-hydroxymethyluracil, is a modification of thymine DNA base involved in RNA Polymerase (Pol) II transcription termination in kinetoplastid protozoa. Little is understood regarding how specific thymine residues are targeted for J-modification or the mechanism of J regulated transcription termination. To identify proteins involved in J-synthesis, we expressed a tagged version of the J-glucosyltransferase (JGT) in Leishmania tarentolae, and identified four co-purified proteins by mass spectrometry: protein phosphatase (PP1), a homolog of Wdr82, a potential PP1 regulatory protein (PNUTS) and a protein containing a J-DNA binding domain (named JBP3). Gel shift studies indicate JBP3 is a J-DNA binding protein. Reciprocal tagging, co-IP and sucrose gradient analyses indicate PP1, JGT, JBP3, Wdr82 and PNUTS form a multimeric complex in kinetoplastids, similar to the mammalian PTW/PP1 complex involved in transcription termination via PP1 mediated dephosphorylation of Pol II. Using RNAi and analysis of Pol II termination by RNA-seq and RT-PCR, we demonstrate that ablation of PNUTS, JBP3 and Wdr82 lead to defects in Pol II termination at the 3'-end of polycistronic gene arrays in Trypanosoma brucei. Mutants also contain increased antisense RNA levels upstream of transcription start sites, suggesting an additional role of the complex in regulating termination of bi-directional transcription. In addition, PNUTS loss causes derepression of silent Variant Surface Glycoprotein genes involved in host immune evasion. Our results suggest a novel mechanistic link between base J and Pol II polycistronic transcription termination in kinetoplastids.

Indexed as

Transcription Termination, GeneticAnimalsDNA-Binding ProteinsDNA, KinetoplastGenes, ProtozoanGlucosidesGlucosyltransferasesHistonesLeishmaniaMutationProtozoan ProteinsRNA InterferenceRNA Polymerase IIThymineTrypanosoma brucei bruceiUracil5-((glucopyranosyloxy)methyl)uracilDNA-Binding ProteinsDNA, KinetoplastGlucosidesGlucosyltransferasesHistonesProtozoan ProteinsRNA Polymerase IIThymineUracil

Identifiers

PMID32084124
PMCPMC7055916
OpenAlexW3007159180

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.