Science AdvancesMolecular BiologyPeer-reviewed journal article
Pronounced sequence specificity of the TET enzyme catalytic domain guides its cellular function
Mirunalini RavichandraniD, Dominik RafalskiiD, Claudia I. DaviesiD, Oscar Ortega‐RecaldeiD, Xinsheng NaniD, Cassandra R. GlanfieldiD, Annika Kötter, Katarzyna MisztaliD, Andrew H. Wang, Marek WojciechowskiiD, Michał RażewiD, Issam M. Mayyas, Olga Kardailsky, Uwe SchwartziD, Krzysztof ZembrzyckiiD, Ian M. MorisoniD, Mark HelmiD, Dieter WeichenhaniD, Renata Zofia JurkowskaiD, Felix KruegeriD, Christoph PlassiD, Martin ZachariasiD, Matthias BochtleriD, Timothy A. HoreiD, Tomasz Piotr JurkowskiiD
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 cores of mammalian TET enzymes favor CpGs embedded within bHLH and bZIP transcription factor binding sites, with 250-fold preference in vitro. Crystal structures and molecular dynamics calculations show that sequence preference is caused by intra-substrate interactions and CpG 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 germline. Most and least favorable TET motifs represent DNA sites that are bound by methylation-sensitive immediate-early transcription factors and OCT4, respectively, illuminating TET function in transcriptional responses and pluripotency support. One-Sentence SummaryThe catalytic domains of the enzymes that facilitate passive and drive active DNA demethylation have intrinsic sequence preferences that target DNA demethylation to bHLH and bZIP transcription factor binding sites.
- organism: mouse
- organism: human
- assay: DNA methylation
- research focus: gene regulatory network inference
- research focus: cell type annotation
- research focus: differential expression
- research focus: protein structure prediction
- approach: statistical model
- approach: experimental assay
- Citations
- 35
- FWCI
- 2.20
- Field percentile
- top 10%
Reproducibility ledger
Nobody has reported trying to reproduce this paper yet. Did you replicate an experiment or run the code? Your report saves the next lab a week.
Sign in to file a reproducibility report.
Related papers
- TET1 Catalytic Activity is Required for Reprogramming of Imprinting Control Regions and Patterning of Sperm-Specific Hypomethylated Regions
Rexxi D. Prasasya, Blake A. Caldwell, … Marisa S. Bartolomei·bioRxiv·Feb 21, 2023
- TET enzymes augment AID expression via 5hmC modifications at the Aicda superenhancer
Chan-Wang J. Lio, Vipul Shukla, … Anjana Rao·bioRxiv·Oct 8, 2018
- Structural basis for activation of DNMT1
A. Kikuchi, H. Onoda, … K. Arita·bioRxiv·Jun 16, 2022
- ZBTB38 requires an extended N-terminal zinc finger network to read mCpG- and discriminate TpG-containing DNA sequences
Jared Boster, Cooper Gangi, … Bethany A. Buck‐Koehntop·Journal of Biological ChemistryPeer-reviewed·Aug 28, 2026
- Flanking sequence preference modulates de novo DNA methylation in the mouse genome
Izaskun Mallona, Ioana Mariuca Ilie, … Tuncay Baubec·Nucleic Acids ResearchPeer-reviewed·Nov 16, 2020
- Identification, expression, and purification of DNA cytosine 5-methyltransferases with short recognition sequences