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Updated: Jun 29, 2025

An Engineered Split-TET2 Enzyme for Chemical-inducible DNA Hydroxymethylation and Epigenetic Remodeling

An Engineered Split-TET2 Enzyme for Chemical-inducible DNA Hydroxymethylation and Epigenetic Remodeling

Published on: December 18, 2017

MLL4 binds TET3.

Dustin C Becht¹, Sk Abdul Mohid², Ji-Eun Lee³

¹Department of Pharmacology, University of Colorado School of Medicine, Aurora, CO 80045, USA.

Structure (London, England : 1993)

|April 5, 2024

Summary

This summary is machine-generated.

Mixed lineage leukemia 4 (MLL4) interacts with ten-eleven translocation 3 (TET3) via its PHD6 finger. This interaction occurs on active enhancers, suggesting a functional link between MLL4 and TET3 in gene regulation.

Keywords:

MLL4 PHD finger TET3 interaction structure

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Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Efficient Purification and LC-MS/MS-based Assay Development for Ten-Eleven Translocation-2 5-Methylcytosine Dioxygenase

Published on: October 15, 2018

Area of Science:

Epigenetics and transcriptional regulation
Protein-protein interactions in gene expression
Biochemistry and structural biology

Background:

Mixed lineage leukemia 4 (MLL4), also known as KMT2D, is crucial for enhancer activation and cell-type specific transcription.
MLL4 possesses a catalytic domain and seven plant homeodomain (PHD) fingers, with limited characterization of the latter.
Ten-eleven translocation 3 (TET3) is a dioxygenase involved in DNA demethylation, converting methylated cytosine to oxidized forms.

Purpose of the Study:

To investigate the interaction between MLL4 and TET3.
To elucidate the structural basis of the MLL4-TET3 binding.
To explore the functional implications of this interaction in gene regulation.

Main Methods:

Solution Nuclear Magnetic Resonance (NMR) structure determination of the TET3-MLL4 PHD6 complex.
Biochemical binding assays to characterize the interaction.
Genomic localization analysis of MLL4 and TET3 in mouse embryonic stem cells.

Main Results:

The sixth PHD finger of MLL4 (MLL4 PHD6) directly binds to a hydrophobic motif on TET3.
Structural analysis reveals TET3 occupies a hydrophobic site on MLL4 PHD6, similar to histone H4.
This interaction is conserved in the seventh PHD finger of MLL3 (MLL3 PHD7).
Endogenous MLL4 and ectopically expressed TET3 show significant overlap in their genomic localization on active enhancers.

Conclusions:

MLL4 PHD6 interacts with TET3 through a conserved hydrophobic binding site.
The overlapping genomic distribution suggests a functional relationship between MLL4 and TET3 at active enhancers.
This interaction may play a role in coordinating epigenetic modifications and DNA demethylation for transcriptional control.