Evidence map›Paper›PMID 24914785›Full record

ArticlePloS one2014

Protozoan ALKBH8 oxygenases display both DNA repair and tRNA modification activities.

Daria Zdżalik, Cathrine B Vågbø, Finn Kirpekar, Erna Davydova, Alicja Puścian, Agnieszka M Maciejewska, Hans E Krokan, Arne Klungland, Barbara Tudek, Erwin van den Born and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 39 citations in OpenAlex.

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  10. Article
  11. Alkbh4 and Atrn Act Maternally to Regulate Zebrafish Epiboly.International journal of biological sciences · 2017
    Article
  12. Complex Relationship between Obesity and the Fat Mass and Obesity Locus.International journal of biological sciences · 2017
    Review
  13. Article
  14. Review
  15. Review
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

11 authors at 5 institutions in 3 countries.

Daria ZdżalikDepartment of Biosciences, University of Oslo, Oslo, Norway; Institute of Genetics and Biotechnology, University of Warsaw, Warsaw, Poland.
Cathrine B VågbøDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway.
Finn KirpekarDepartment of Biochemistry and Molecular Biology, University of Southern Denmark, Odense, Denmark.
Erna DavydovaDepartment of Biosciences, University of Oslo, Oslo, Norway.
Alicja PuścianInstitute of Genetics and Biotechnology, University of Warsaw, Warsaw, Poland; Department of Neurophysiology, Nencki Institute of Experimental Biology, Polish Academy of Sciences, Warsaw, Poland.
Agnieszka M MaciejewskaInstitute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Hans E KrokanDepartment of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, Trondheim, Norway.
Arne KlunglandClinic for Diagnostics and Intervention and Institute of Medical Microbiology, Oslo University Hospital, Rikshospitalet, Oslo, Norway; Institute of Basic Medical Sciences, University of Oslo, Oslo, Norway.
Barbara TudekInstitute of Genetics and Biotechnology, University of Warsaw, Warsaw, Poland; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Erwin van den BornDepartment of Biosciences, University of Oslo, Oslo, Norway.
Pål Ø FalnesDepartment of Biosciences, University of Oslo, Oslo, Norway.
University of Oslo · NOInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLNorwegian University of Science and Technology · NOUniversity of Southern Denmark · DKUniversity of Warsaw · PL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ALKBH family of Fe(II) and 2-oxoglutarate dependent oxygenases comprises enzymes that display sequence homology to AlkB from E. coli, a DNA repair enzyme that uses an oxidative mechanism to dealkylate methyl and etheno adducts on the nucleobases. Humans have nine different ALKBH proteins, ALKBH1-8 and FTO. Mammalian and plant ALKBH8 are tRNA hydroxylases targeting 5-methoxycarbonylmethyl-modified uridine (mcm5U) at the wobble position of tRNAGly(UCC). In contrast, the genomes of some bacteria encode a protein with strong sequence homology to ALKBH8, and robust DNA repair activity was previously demonstrated for one such protein. To further explore this apparent functional duality of the ALKBH8 proteins, we have here enzymatically characterized a panel of such proteins, originating from bacteria, protozoa and mimivirus. All the enzymes showed DNA repair activity in vitro, but, interestingly, two protozoan ALKBH8s also catalyzed wobble uridine modification of tRNA, thus displaying a dual in vitro activity. Also, we found the modification status of tRNAGly(UCC) to be unaltered in an ALKBH8 deficient mutant of Agrobacterium tumefaciens, indicating that bacterial ALKBH8s have a function different from that of their eukaryotic counterparts. The present study provides new insights on the function and evolution of the ALKBH8 family of proteins.

Indexed as

DNA RepairAgrobacterium tumefaciensAmino Acid SequenceComputational BiologyDioxygenasesDNA DamageDNA MethylationEnzyme ActivationHumansMolecular Sequence DataMutationProtozoan ProteinsRecombinant ProteinsRNA, TransferSequence AlignmenttRNA MethyltransferasesDioxygenasesProtozoan ProteinsRecombinant ProteinsRNA, TransfertRNA Methyltransferases

Identifiers

PMID24914785
PMCPMC4051686
OpenAlexW1999202913

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Registered trials

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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.