Evidence map›Paper›PMID 36070377›Full record

ArticleScience advances2022

Pronounced sequence specificity of the TET enzyme catalytic domain guides its cellular function.

Mirunalini Ravichandran, Dominik Rafalski, Claudia I Davies, Oscar Ortega-Recalde, Xinsheng Nan, Cassandra R Glanfield, Annika Kotter, Katarzyna Misztal, Andrew H Wang, Marek Wojciechowski and 15 more

Open access · goldAbstract read
In one paragraph

Article in Science advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
3.1field-weighted citation impact, top 7% 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, 36 citations in OpenAlex.

  1. Article
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  3. 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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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

25 authors at 10 institutions in 5 countries.

Mirunalini RavichandranDepartment of Anatomy, University of California, San Francisco, 513 Parnassus Avenue, HSW 1301, San Francisco, CA 94143, USA.ORCID 0000-0002-1991-5695
Dominik RafalskiInternational Institute of Molecular and Cell Biology in Warsaw (IIMCB), Trojdena 4, 02-109 Warsaw, Poland.ORCID 0000-0002-3449-7460
Claudia I DaviesUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.ORCID 0000-0001-7416-3249
Oscar Ortega-RecaldeUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.ORCID 0000-0002-8076-0346
Xinsheng NanCardiff University, School of Biosciences, Museum Avenue, CF10 3AX Cardiff, Wales, UK.ORCID 0000-0002-0865-7934
Cassandra R GlanfieldUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.ORCID 0000-0002-2049-8585
Annika KotterJohannes-Gutenberg-Universität Mainz, Institute of Pharmaceutical and Biomedical Sciences, Staudingerweg 5, 55128 Mainz, Germany.
Katarzyna MisztalInternational Institute of Molecular and Cell Biology in Warsaw (IIMCB), Trojdena 4, 02-109 Warsaw, Poland.ORCID 0000-0001-6575-2500
Andrew H WangUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.
Marek WojciechowskiInternational Institute of Molecular and Cell Biology in Warsaw (IIMCB), Trojdena 4, 02-109 Warsaw, Poland.ORCID 0000-0002-8935-3640
Michał RażewInternational Institute of Molecular and Cell Biology in Warsaw (IIMCB), Trojdena 4, 02-109 Warsaw, Poland.ORCID 0000-0003-1306-4743
Issam M MayyasUniversity of Otago, Department of Pathology, Dunedin 9016, New Zealand.
Olga KardailskyUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.
Uwe SchwartzUniversity of Regensburg, Computational Core Unit, 93053 Regensburg, Germany.ORCID 0000-0002-7628-2687
Krzysztof ZembrzyckiInstitute of Fundamental Technological Research, Department of Biosystems and Soft Matter PAS, Pawińskiego 5B, Warsaw, Poland.ORCID 0000-0001-7693-174X
Ian M MorisonUniversity of Otago, Department of Pathology, Dunedin 9016, New Zealand.ORCID 0000-0003-3616-0025
Mark HelmJohannes-Gutenberg-Universität Mainz, Institute of Pharmaceutical and Biomedical Sciences, Staudingerweg 5, 55128 Mainz, Germany.ORCID 0000-0002-0154-0928
Dieter WeichenhanGerman Cancer Research Center (DKFZ), Division of Cancer Epigenomics, Heidelberg, Germany.
Renata Z JurkowskaCardiff University, School of Biosciences, Museum Avenue, CF10 3AX Cardiff, Wales, UK.ORCID 0000-0002-4507-2222
Felix KruegerBioinformatics Group, The Babraham Institute, Cambridge CB22 3AT, UK.ORCID 0000-0002-5513-3324
Christoph PlassGerman Cancer Research Center (DKFZ), Division of Cancer Epigenomics, Heidelberg, Germany.ORCID 0000-0003-2554-3952
Martin ZachariasPhysics Department, Technical University of Munich, James-Franck Str. 1, 85748 Garching, Germany.ORCID 0000-0001-5163-2663
Matthias BochtlerInternational Institute of Molecular and Cell Biology in Warsaw (IIMCB), Trojdena 4, 02-109 Warsaw, Poland.ORCID 0000-0001-7884-4463
Timothy A HoreUniversity of Otago, Department of Anatomy, Dunedin 9016, New Zealand.ORCID 0000-0002-6735-225X
Tomasz P JurkowskiUniversität Stuttgart, Abteilung Biochemie, Institute für Biochemie und Technische Biochemie, Allmandring 31, Stuttgart D-70569, Germany.ORCID 0000-0002-2012-0240
University of Otago · NZInternational Institute of Molecular and Cell Biology · PLCardiff University · GBGerman Cancer Research Center · DEJohannes Gutenberg University Mainz · DEUniversity of Stuttgart · DEBabraham Institute · GBInstitute of Fundamental Technological Research · PLTechnical University of Munich · DEUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TET (ten-eleven translocation) enzymes catalyze the oxidation of 5-methylcytosine bases in DNA, thus driving active and passive DNA demethylation. Here, we report that the catalytic domain of mammalian TET enzymes favor CGs embedded within basic helix-loop-helix and basic leucine zipper domain transcription factor-binding sites, with up to 250-fold preference in vitro. Crystal structures and molecular dynamics calculations show that sequence preference is caused by intrasubstrate interactions and CG flanking sequence indirectly affecting enzyme conformation. TET sequence preferences are physiologically relevant as they explain the rates of DNA demethylation in TET-rescue experiments in culture and in vivo within the zygote and germ line. Most and least favorable TET motifs represent DNA sites that are bound by methylation-sensitive immediate-early transcription factors and octamer-binding transcription factor 4 (OCT4), respectively, illuminating TET function in transcriptional responses and pluripotency support.

Indexed as

5-MethylcytosineDioxygenasesAnimalsCatalytic DomainCell Physiological PhenomenaDNAMammals5-MethylcytosineDioxygenasesDNA

Identifiers

PMID36070377
PMCPMC9451156
OpenAlexW4294884846

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.