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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

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The L3MBTL3 Methyl-Lysine Reader Domain Functions As a Dimer.

Brandi M Baughman¹, Samantha G Pattenden¹, Jacqueline L Norris¹

¹Center for Integrative Chemical Biology and Drug Discovery, Division of Chemical Biology and Medicinal Chemistry, UNC Eshelman School of Pharmacy, University of North Carolina at Chapel Hill , Chapel Hill, North Carolina 27599, United States.

ACS Chemical Biology

|August 29, 2015

Summary

L3MBTL3 protein functions as a dimer to bind methylated histone tails. Mutations in its MBT domains disrupt this crucial dimerization in cells and in vitro.

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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

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Area of Science:

Biochemistry
Molecular Biology
Epigenetics

Background:

L3MBTL3 protein recognizes specific histone modifications, specifically mono- and dimethylated lysine residues.
Previous studies revealed a 2:2 dimer structure of L3MBTL3 bound to small molecules, suggesting a dimerization-dependent recognition mechanism.

Purpose of the Study:

To investigate the dimerization of L3MBTL3 protein through its MBT domains.
To determine if L3MBTL3 dimerization occurs in a cellular environment without small molecule ligands.
To assess the impact of mutations in the MBT domains on L3MBTL3 dimerization.

Main Methods:

In vitro dimerization assays of L3MBTL3 protein.
Cellular analysis of L3MBTL3 dimerization.
Site-directed mutagenesis of the first and second MBT domains of L3MBTL3.

Main Results:

L3MBTL3 protein undergoes dimerization via its MBT domains.
Dimerization of L3MBTL3 was confirmed within a cellular context, independent of small molecule ligands.
Mutations in the first and second MBT domains abolished L3MBTL3 dimerization both in vitro and in cells.

Conclusions:

L3MBTL3 engages methylated histone tails as a dimer, supporting its functional mechanism.
The observed dimerization explains the evolutionary presence of repeated MBT domains within L3MBTL3.
MBT domain-mediated dimerization is essential for L3MBTL3's biological function.