Evidence map›Paper›PMID 19136460›Full record

ArticleNucleic acids research2009

JBP1 and JBP2 are two distinct thymidine hydroxylases involved in J biosynthesis in genomic DNA of African trypanosomes.

Laura J Cliffe, Rudo Kieft, Timothy Southern, Shanda R Birkeland, Marion Marshall, Kate Sweeney, Robert Sabatini

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.1field-weighted citation impact, top 6% 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

52 citing papers in PubMed, 90 citations in OpenAlex.

  1. Uncovering ParB-dependent and -independent subclasses of T-dioxygenases from bacteriophage.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  9. Structure and Function of TET Enzymes.Advances in experimental medicine and biology · 2022
    Article
  10. Phage-encoded ten-eleven translocation dioxygenase (TET) is active in C5-cytosine hypermodification in DNA.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  11. Article
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  14. Article
  15. Identification ofMolecules (Basel, Switzerland) · 2019
    Article
  16. Journal of parasitic diseases : official organ of the Indian Society for Parasitology · 2019
    Article
  17. Review
  18. Review
  19. Article
  20. Article
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

7 authors at 1 institution in 1 country.

Laura J CliffeDepartment of Biochemistry and Molecular Biology, University of Georgia, Athens, Georgia 30602, USA.
Rudo Kieft
Timothy Southern
Shanda R Birkeland
Marion Marshall
Kate Sweeney
Robert Sabatini
University of Georgia · US

Funding

Biosynthesis and Function of Base JR01AI063523 · NIAID · UNIVERSITY OF GEORGIA · PI SABATINI, ROBERT S · 2006 to 2010
$1.6M
Biosynthesis and function of base J in T. bruceiR56AI063523 · NIAID · UNIVERSITY OF GEORGIA · PI SABATINI, ROBERT S · 2011 to 2011
$384k
NIAID NIH HHS AI063523NIAID NIH HHS R01 AI063523NIAID NIH HHS R56 AI063523
6 · The paper itself

Abstract

Genomic DNA of African trypanosomes contains a hypermodified thymidine residue termed base J (beta-d-glucosyl-HOMedU). This modified base is localized primarily to repetitive DNA, namely the telomeres, and is implicated in the regulation of antigenic variation. The base is synthesized in a two-step pathway. Initially, a thymidine residue in DNA is hydroxylated by a thymidine hydroxylase (TH). This intermediate (HOMedU) is then glucosylated to form base J. Two proteins involved in J synthesis, JBP1 (J binding protein 1) and JBP2, contain a putative TH domain related to the family of Fe(2+)/2-oxoglutarate-dependent hydroxylases. We have previously shown that mutations in the TH domain of JBP1 kill its ability to stimulate J synthesis. Here we show that mutation of key residues in the TH domain of JBP2 ablate its ability to induce de novo J synthesis. While the individual JBP1 null and JBP2 null trypanosomes have reduced J levels, the deletion of both JBP1 and JBP2 generates a cell line that completely lacks base J but still contains glucosyl-transferase activity. Reintroduction of JBP2 in the J-null trypanosome stimulates HOMedU formation and site-specific synthesis of base J. We conclude that JBP2 and JBP1 are the TH enzymes involved in J biosynthesis.

Indexed as

AnimalsCell LineDNA-Binding ProteinsDNA, ProtozoanGene DeletionGenome, ProtozoanGlucosidesMixed Function OxygenasesMutationProtein Structure, TertiaryProtozoan ProteinsTrypanosoma brucei bruceiUracil5-((glucopyranosyloxy)methyl)uracilDNA-Binding ProteinsDNA, ProtozoanGlucosidesJ-binding protein, Trypanosoma bruceiMixed Function OxygenasesProtozoan Proteinsthymidine,2-oxoglutarate dioxygenaseUracil

Identifiers

PMID19136460
PMCPMC2655668
OpenAlexW2105761530

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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.