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TitleMolecular basis for the inhibition of de novo DNA methylation by TCL1A.
Journal, issue, pagesNat Commun, Vol. 17, Issue 1, Year 2026
Publish dateMar 5, 2026
AuthorsQingting Liu / Jinhong Li / Xiaoxiao Wang / Yaozong Li / Yu Wu / Zhuo Han / Zixin Guo / Li Guo / Xiang Wang / Gang Yuan / Zheng Gao / Lei Li / Dong Deng /
PubMed AbstractDNA methyltransferases DNMT3A/B mediate de novo DNA methylation, essential for embryonic development and cell fate determination. Dysregulation of DNMT3A/B causes developmental defects and ...DNA methyltransferases DNMT3A/B mediate de novo DNA methylation, essential for embryonic development and cell fate determination. Dysregulation of DNMT3A/B causes developmental defects and tumorigenesis. TCL1A is critical for embryogenesis but promotes lymphomagenesis when deregulated. Previous studies suggested TCL1A binds DNMT3A/B and inhibits their activity, but the mechanism remained unclear. Here, we report the cryo-EM structure of the DNMT3A-TCL1A complex, which comprises a DNMT3A dimer bound by two TCL1A dimers. TCL1A interacts with the catalytic domain of DNMT3A, overlapping with the DNMT3L-binding site, and induces extended conformational rearrangements. The target recognition domain and catalytic loop shift markedly, reducing DNA accessibility, while the catalytic loop occupies the SAM-binding pocket, thereby blocking methyltransferase activity. Supported by biochemical assays and molecular dynamics simulations, we propose a dynamic inhibition mechanism in which TCL1A exploits DNMT3A conformational plasticity to suppress de novo DNA methylation.
External linksNat Commun / PubMed:41786706 / PubMed Central
MethodsEM (single particle)
Resolution3.36 Å
Structure data

63290

9lq1

EMDB-63290, PDB-9lq1:
Structure of human DNMT3A-TCL1A complex
Method: EM (single particle) / Resolution: 3.36 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSFERASE / complex

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