Tet Enzymes, Variants, and Differential Effects on Function
Open accessAbstract
Discovery of the ten-eleven translocation 1 (TET) methylcytosine dioxygenase family of enzymes, nearly 10 years ago, heralded a major breakthrough in understanding the epigenetic modifications of DNA. Initially described as catalyzing the oxidation of methyl cytosine (5mC) to hydroxymethyl cytosine (5hmC), it is now clear that these enzymes can also catalyze additional reactions leading to active DNA demethylation. The association of TET enzymes, as well as the 5hmC, with active regulatory regions of the genome has been studied extensively in embryonic stem cells, although these enzymes are expressed widely also in differentiated tissues. However TET1 and TET3 are found as various isoforms, as a result of utilizing alternative regulatory regions in distinct tissues. Some of these isoforms, like TET2, lack the CXXC domain which probably has major implications on their recruitment to specific loci in the genome, while in certain contexts TET1 is seen paradoxically to repress transcription. In this review we bring together these novel aspects of the differential regulation of these Tet isoforms and the likely consequences on their activity.
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In mammals, DNMT1 has been identified as de novo methyltransferase, whereas DNMT3A and DNMT3B are maintenance methyltransferases.
“In mammals, DNMT1 has been identified as de novo methyltransferase, whereas DNMT3A and DNMT3B are maintenance methyltransferases.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
In “The TET enzymes, DNA hydroxymethylation, and demethylation” (page unavailable), the paper says DNMT1 is recruited to hemimethylated CpG during DNA replication, contrary to the claim’s assignment of DNMT1 to de novo methylation. Its References section (page unavailable) also identifies DNMT1 as a maintenance methyltransferase. The retrieved passages do not address the claimed roles of DNMT3A and DNMT3B. (LLM, conf=0.86)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredMethylation or demethylation in histones results in activation or inhibition of gene expression, respectively, by modulating DNA access to transcription factors through relaxation or compaction of chromatin structure.
“Methylation or demethylation in histones results in the activation or inhibition of gene expression, respectively, by modulating DNA access to transcription factors through relaxation or compaction of the chromatin structure [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
In “Different effects of different isoforms?” (page unavailable), the paper links H3K27 histone methylation to repression of the Lhb gene, contrary to the claim that histone methylation activates expression. It also associates H3K36 methylation with active transcription, so it does not present methylation and demethylation as having the fixed, opposing effects claimed. (LLM, conf=0.84)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredTET enzymes (10-11 translocases), which are monooxygenases, mediate sequential oxidation of 5mC, and together with single-base excision, DNA repair machinery, and thymine DNA glycosylase (TDG) demethylases DNA.
“On the other hand, a group of enzymes called TET (10–11 translocases), which are monooxygenases, mediate the sequential oxidation of 5mC, and together with single-base excision, DNA repair machinery, and thymine DNA, glycosylase (TDG) demethylases DNA [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section “The TET enzymes, DNA hydroxymethylation, and demethylation” describes sequential oxidation of 5mC, followed by TDG excision and base excision repair to complete active demethylation. However, it calls TET enzymes ten-eleven translocation methylcytosine dioxygenases, not “translocases” or monooxygenases. (LLM, conf=0.90)
Experimental — accuracy not yet measuredHistone methylation occurs in lysine and arginine residues in histone tails, where histone methyltransferases transfer a methyl group from SAM; demethylation is orchestrated by histone demethylases.
“Histone methylation occurs in lysine and arginine residues in histone tails, where histone methyltransferases transfer to a methyl group from a donor, SAM; demethylation is orchestrated by histone demethylases.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
In “Different effects of different isoforms?” (page unavailable), the paper mentions H3K36 methyltransferases and their enzymatic activity, providing limited support for histone methylation by methyltransferases. It does not describe arginine methylation, SAM as the methyl donor, or histone demethylases; its demethylation discussion concerns DNA cytosine instead. (LLM, conf=0.78)
Experimental — accuracy not yet measuredDNA methylation is regulated by DNA methyltransferases (DNMTs), which catalyze transfer of a methyl group from S-adenosylmethionine (SAM) to cytokines.
“Given its reversible nature, DNA methylation is regulated by DNA methyltransferases (DNMTs), which catalyze the transfer of a methyl group from a donor group called S-adenosylmethionine (SAM) to cytokines.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section “The TET enzymes, DNA hydroxymethylation, and demethylation” describes DNMT1 acting at hemimethylated DNA sites, supporting the DNMT connection to methylation. It does not describe SAM as the methyl donor or the claimed transfer reaction. The paper discusses cytosines, not cytokines, as the DNA bases involved. (LLM, conf=0.82)
Experimental — accuracy not yet measured
Marks on histone tails act as recognition signals for proteins and chromatin regulatory complexes.
“In this sense, the marks on the histone tails would be like a recognition signal for proteins and chromatin regulatory complexes.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
In “The TET enzymes, DNA hydroxymethylation, and demethylation” (page unavailable), the paper says that the DNA mark 5hmC can recruit or displace proteins. “Different effects of different isoforms?” (page unavailable) also describes a regulatory complex binding 5hmC-modified DNA. These passages support the recognition-signal idea for DNA marks, but not the claim’s specific reference to marks on histone tails. (LLM, conf=0.78)
Experimental — accuracy not yet measuredAcetylation is involved in recognition of acetylation marks on histones by different proteins which can recruit different classes of chromatin structures, regulating proteins to promote or inhibit gene transcription.
“And secondly, it is involved in the recognition of acetylation marks on histones by different proteins which can recruit different classes of chromatin structures, regulating proteins to promote or inhibit gene transcription [55,58].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section on TET enzymes and DNA hydroxymethylation describes proteins recognizing 5hmC-modified DNA and altering the chromatin environment, not recognizing acetylation marks on histones. The section on regulation of TET expression mentions acetylation of TET enzymes, but does not address the claimed histone-acetylation mechanism. Searches for histone-acetylation recognition and bromodomains found no passage supporting it. (LLM, conf=0.78)
Experimental — accuracy not yet measuredDeacetylases remove acetyl groups of acetylated lysine.
“On the other hand, the deacetylases remove acetyl groups of acetylated lysine.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section ‘The TET enzymes, DNA hydroxymethylation, and demethylation’ describes removal of modified cytosines during DNA demethylation, not removal of acetyl groups from lysine. Searches for deacetylases and acetylated lysine found no passage in our copy addressing the claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredAcetylation neutralizes the positive charge of lysine by adding the acetyl group to histones, forming an affinity between DNA and histones less tightly arranged, and consequently greater accessibility of DNA to transcription factors.
“Firstly, it refers to the ability to neutralize the positive charge of the lysine by adding the acetyl group to histones, thus forming an affinity between DNA (negatively charged) and histones less tightly arranged, and consequently, greater accessibility of DNA to transcription factors is observed, for example.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section ‘The TET enzymes, DNA hydroxymethylation, and demethylation’ discusses DNA hydroxymethylation and its association with transcription, not histone acetylation. Searches for lysine charge neutralization, weakened DNA–histone binding, and transcription-factor accessibility found no passage addressing the claimed mechanism; page numbers were unavailable in our copy. (LLM, conf=0.76)
Experimental — accuracy not yet measuredAcetylation occurs in N-terminal lysine residues of histones and is mediated by acetyltransferases (HATs) that add acetyl groups to histone tails.
“Acetylation occurs in the N-terminal lysine residues of histones, and this mechanism is mediated by acetyltransferases (HATs) that are responsible for adding acetyl groups to the tails of histones.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section “The TET enzymes, DNA hydroxymethylation, and demethylation” describes TET-mediated DNA modification, not histone acetylation (page unavailable). Searches for HATs, N-terminal histone lysines, and acetylation of histone tails found no passage in our copy addressing the claim. (LLM, conf=0.76)
Experimental — accuracy not yet measuredAcetylation in tail histones plays an important role during transcription regulation through two mechanisms.
“This modification in tail histones plays a very important role during transcription regulation through two mechanisms.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section “The TET enzymes, DNA hydroxymethylation, and demethylation” discusses DNA hydroxymethylation and its relationship to transcription, not histone-tail acetylation. Searches for histone-tail acetylation and its proposed two mechanisms found no passage addressing the attributed claim; the paper’s discussion of other modifications does not contradict it. (LLM, conf=0.76)
Experimental — accuracy not yet measuredHistone codes mediate transcriptional inhibition or activation, leading to many biological effects.
“The histone codes are involved in cell differentiation, cell mitosis, the repair of DNA damage, and X chromatin inactivation, and mediate transcriptional inhibition or activation, leading to many biological effects [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The sections on TET enzymes and differential isoform effects discuss DNA hydroxymethylation and TET-mediated transcriptional regulation, not histone codes. Searches for histone codes and the claimed roles in differentiation, mitosis, DNA-damage repair, and X-chromatin inactivation found no passage addressing the attributed claim. (LLM, conf=0.72)
Experimental — accuracy not yet measuredPost-translational modifications in the amino acids of histone tails are recognized as the histone code, which can affect the accessibility of different proteins to DNA.
“Post-translational modifications in the amino acids of the histone tails are recognized as the histone code, which can affect the accessibility of different proteins to the DNA.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section on TET enzymes and DNA hydroxymethylation says that modification of DNA can change which proteins bind, but it does not address modifications of histone tails or define a histone code. Searches for those terms and for histone modifications affecting protein access to DNA found no passage supporting the attributed claim. No page number is available in our copy. (LLM, conf=0.74)
Experimental — accuracy not yet measuredInformation contained in the histone code could be inherited by daughter cells after DNA replication.
“In this way, the different combinations observed in histone tails can vary between nucleosomes, and the information contained in the code could be inherited by daughter cells after DNA replication [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section “The TET enzymes, DNA hydroxymethylation, and demethylation” (page unavailable) discusses DNA cytosine modifications, including changes during replication, but does not address inheritance of the histone code by daughter cells. Searches for histone-code inheritance and histone-tail modifications after replication found no passage addressing the claim. (LLM, conf=0.72)
Experimental — accuracy not yet measuredThe histone code impacts the structure of euchromatin and heterochromatin.
“This code also has an impact on the structure of euchromatin and heterochromatin.”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section on TET enzymes and DNA hydroxymethylation says that the DNA mark 5hmC probably alters the local chromatin environment. The passages searched for “histone code” and histone modifications do not address whether the histone code affects the structure of both euchromatin and heterochromatin. (LLM, conf=0.73)
Experimental — accuracy not yet measuredHistone codes are involved in cell differentiation, cell mitosis, the repair of DNA damage, and X chromatin inactivation.
“The histone codes are involved in cell differentiation, cell mitosis, the repair of DNA damage, and X chromatin inactivation, and mediate transcriptional inhibition or activation, leading to many biological effects [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The sections on TET enzymes and on different isoforms discuss DNA hydroxymethylation, differentiation, and TET1-mediated transcriptional repression; the latter also mentions an H3K27 histone mark. Searches for “histone code,” mitosis, DNA-damage repair, and X-chromatin inactivation found no passage attributing the listed functions to histone codes. The cited paper therefore does not verify this claim. (LLM, conf=0.73)
Experimental — accuracy not yet measuredDifferent combinations observed in histone tails can vary between nucleosomes.
“In this way, the different combinations observed in histone tails can vary between nucleosomes, and the information contained in the code could be inherited by daughter cells after DNA replication [55].”
From Revisiting Epigenetics Fundamentals and Its Biomedical Implications (2024) · cites this paper as [55]
The section on TET enzymes, DNA hydroxymethylation, and demethylation discusses modifications of DNA, not combinations of modifications on histone tails across nucleosomes (page not provided). Searches for histone-tail combinations and the histone code found no passage in our copy addressing the attributed claim. (LLM, conf=0.73)
Experimental — accuracy not yet measured
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Cytosine Modifications and Distinct Functions of TET1 on Tumorigenesis
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Gerdy, V., Auxerre-Plantié, E., Bertrand, R., Renaud, Y., Junion, G., Vandel, L., & Waltzer, L. (2025) · Skeletal Muscle · doi:10.1186/s13395-025-00399-x · Cited by 2 · see citing works
Enkhmandakh, B., Joshi, P., Robson, P., Vijaykumar, A., Mina, M., Shin, D., & Bayarsaihan, D. (2023) · The Cleft Palate-Craniofacial Journal · doi:10.1177/10556656231172296 · Cited by 2 · see citing works
Ghasemi, B., Ahmadi, J., Zaker, F., Tabatabaei, T., Kiani-Zadeh, M., & Kazemi, A. (2023) · Indian Journal of Hematology and Blood Transfusion · doi:10.1007/s12288-023-01673-y · Cited by 2 · see citing works
Kouidou, S., Malousi, A., & Andreou, A. Z. (2020) · Pathogens · doi:10.3390/pathogens9121006 · Cited by 2 · see citing works
TET2 Promotes Keloid Hyperplasia by Regulating 5hmC Modification in the TGFβ Promoter Region
Niu, C., & Tan, S. (2023) · Clinical Cosmetic and Investigational Dermatology · doi:10.2147/ccid.s409621 · Cited by 2 · see citing works
The regulation mechanisms and the Lamarckian inheritance property of DNA methylation in animals
Li, Y., Xu, Y., Liu, T., Chang, H., & Yang, X. (2021) · Mammalian Genome · doi:10.1007/s00335-021-09870-8 · Cited by 2 · see citing works
Epigenetic Enzymes and Their Mutations in Cancer
Dalmızrak, A., & Dalmızrak, Ö. (2023) · Epigenetics and human health · doi:10.1007/978-3-031-42365-9_2 · Cited by 1 · see citing works
Targeting Epigenetic Readers Using Small Molecule Binders and PROTAC Degraders
Boccia, E., Gazzillo, E., Chini, M. G., Bifulco, G., & Lauro, G. (2024) · Interdisciplinary cancer research · doi:10.1007/16833_2024_240 · Cited by 1 · see citing works
Agu, P. C., & Aja, P. M. (2025) · Toxicological & Environmental Chemistry Reviews · doi:10.1080/02772248.2025.2527656 · Cited by 1 · see citing works
TET enzymes and key signalling pathways: Crosstalk in embryonic development and cancer
Salomão, K. B., Cruzeiro, G. A. V., Chagas, P. S., Bonfim-Silva, R., Brassesco, M. S., & Tone, L. G. (2019) · Integrative Cancer Science and Therapeutics · doi:10.15761/icst.1000318 · Cited by 1 · see citing works
Peptide-based inhibitors of epigenetic proteins
Hintzen, J. C. J., & Mecinović, J. (2024) · Progress in molecular biology and translational science · doi:10.1016/bs.pmbts.2024.04.004 · Cited by 1 · see citing works
- Authors
- Melamed, P., Yosefzon, Y., David, C., Tsukerman, A., & Pnueli, L.
- Affiliations
- Technion – Israel Institute of Technology (IL)
- Corresponding author
- Melamed, Philippa
- Venue
- Frontiers in Cell and Developmental Biology
- Publisher
- Frontiers Media SA
- Published
- 2018-03-05
- Volume
- 6
- Pages
- 22-22
- ISSN
- 2296-634X (ISSN-L)
- PMC
- PMC5844914
- OpenAlex
- W2790004746
- Cited by
- 130
- References
- 56
- Citations by year
- 2026: 10 · 2025: 10 · 2024: 10 · 2023: 19 · 2022: 26 · 2021: 14 · 2020: 25 · 2019: 10 · 2018: 6
- FWCI
- 1.35
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Frontiers in Cell and Developmental Biology (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- Deutsche Forschungsgemeinschaft (BO 1743/7-1)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Epigenetics and DNA Methylation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Keywords
- TET enzymes, 5-methylcytosine oxidation, 5-hydroxymethylcytosine, DNA demethylation, TET1, TET2, TET3, CXXC domain, alternative splicing, transcriptional repression, epigenetic regulation, embryonic stem cells
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