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Related Concept Videos

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This protocol illustrates a chemically induced protein dimerization system to create condensates on chromatin.  The formation of promyelocytic leukemia (PML) nuclear body on telomeres with chemical dimerizers is demonstrated. Droplet growth, dissolution, localization and composition are monitored with live cell imaging, immunofluorescence (IF) and fluorescence in situ hybridization...
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Creating chemically induced protein dimerization systems with desired affinity and specificity for any given small molecule ligand would have many biological sensing and actuation applications. Here, we describe an efficient, generalizable method for de novo engineering of chemically induced dimerization systems via the stepwise selection of a phage-displayed combinatorial single-domain antibody...
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Related Experiment Video

Updated: Jan 20, 2026

Chemical Dimerization-Induced Protein Condensates on Telomeres
08:52

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Modular Thermal Control of Protein Dimerization.

Dan I Piraner, Yan Wu, Mikhail G Shapiro

    ACS Synthetic Biology
    |September 7, 2019
    PubMed
    Summary
    This summary is machine-generated.

    Researchers developed "thermomers," temperature-controlled protein domains. This innovation allows precise, remote control of protein interactions within cells for biological research and therapies.

    Keywords:
    coiled-coilsmammalian synthetic biologyprotein localizationtemperaturethermal controlthermomers

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    Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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    Standardized Modular Assembly of Polycistronic Operons with Modular Cloning (MoClo) using the In-Cloning toolkit

    Published on: September 2, 2025

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    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Biotechnology

    Background:

    • Protein-protein interactions and localization are crucial for cellular signaling.
    • External control methods like chemical and optogenetics have limitations in spatiotemporal specificity, especially in complex tissues.
    • Existing methods struggle with precise control in light-scattering biological environments.

    Purpose of the Study:

    • To introduce a novel method for controlling protein-protein interactions using temperature.
    • To overcome the spatiotemporal limitations of current chemical and optogenetic control techniques.
    • To engineer a versatile tool for biological research, cell-based therapies, and engineered materials.

    Main Methods:

    • Development of "thermomers," modular protein dimerization domains based on a thermolabile coiled-coil protein.
    • Engineering the protein to heterodimerize within a tunable, biocompatible temperature range (37-42 °C).
    • Fusion of thermomers to target proteins to control their association and localization, demonstrated via mammalian cell membrane localization.

    Main Results:

    • Demonstrated reversible control of protein association and localization using thermomers.
    • Achieved precise spatiotemporal control of intracellular protein-protein interactions via temperature.
    • Successfully engineered thermomers to function within the physiological temperature range.

    Conclusions:

    • Thermomers offer a novel, temperature-based approach to control protein-protein interactions with high spatiotemporal precision.
    • This technology overcomes limitations of existing methods in scattering tissues and diverse biological contexts.
    • Thermomers provide a versatile platform for applications in biological research, therapeutic interventions, and living material engineering.