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Author Spotlight: Evaluating Biophysical Assays for Characterizing PROTACS Ternary Complexes

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Complexoform-restricted covalent TRMT112 ligands that allosterically agonize METTL5.

F Wieland Goetzke¹, Steffen M Bernard², Cheng-Wei Ju^3,4,5

¹Department of Chemistry, Scripps Research, La Jolla, CA, USA. fgoetzke@scripps.edu.

Nature Chemical Biology

|January 8, 2026

Summary

Researchers developed chemical probes to specifically target the TRMT112 adaptor protein when it interacts with METTL5. This approach allows for partner-specific functional effects, overcoming challenges in studying adaptable proteins.

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Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

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Published on: February 28, 2025

Area of Science:

Chemical Biology
Molecular Cell Biology
Protein Biochemistry

Background:

Adaptor proteins regulate multiple protein complexes, complicating their study due to pleiotropic effects upon genetic disruption.
TRMT112 is a methyltransferase (MT) adaptor involved in various cellular functions through distinct complexoforms.

Purpose of the Study:

To develop chemical proteomic tools for studying adaptor protein complexoforms.
To investigate the specific interactions of TRMT112 with methyltransferases (MTs).

Main Methods:

Chemical proteomic discovery of bicyclopyrrolidine acrylamide stereoprobes.
Assessing stereoprobe reactivity with recombinant TRMT112 and its complexes with MTs.
Cocrystallography to determine the binding mode of stereoprobes.

Main Results:

Stereoprobes selectively reacted with TRMT112 in the presence of METTL5, but not with uncomplexed TRMT112 or other TRMT112:MT complexes.
Cocrystal structure revealed a composite binding pocket templated by METTL5.
Stereoprobe binding induced allosteric agonism of METTL5 activity.

Conclusions:

Covalent ligands can achieve partner-specific functional effects by targeting unique adaptor complexoforms.
This study provides a novel chemical biology approach to dissect adaptor protein functions in a complexoform-specific manner.