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Related Concept Videos

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Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked.  In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
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Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
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Related Experiment Video

Updated: Jul 12, 2025

Creating Highly Specific Chemically Induced Protein Dimerization Systems by Stepwise Phage Selection of a Combinatorial Single-Domain Antibody Library
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An orthogonalized PYR1-based CID module with reprogrammable ligand-binding specificity.

Sang-Youl Park1,2, Jingde Qiu1,2, Shuang Wei3

  • 1Department of Botany and Plant Sciences, University of California, Riverside, Riverside, CA, USA.

Nature Chemical Biology
|October 23, 2023
PubMed
Summary
This summary is machine-generated.

Scientists engineered new chemical-induced dimerization (CID) modules to reprogram plant hormone (abscisic acid) receptors. This innovation enables sensitive detection of contaminants using living biosensors and synthetic biology applications.

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Area of Science:

  • Synthetic Biology
  • Molecular Biology
  • Plant Science

Background:

  • Plants utilize abscisic acid (ABA) signaling pathways involving receptors like PYR1 and phosphatases like HAB1.
  • The PYR1 receptor system allows for reprogramming of ligand recognition, offering unique synthetic biology potential.
  • Existing systems lack orthogonality and multi-channel capabilities for complex sensing applications.

Purpose of the Study:

  • To design and validate an orthogonal chemical-induced dimerization (CID) module to expand the PYR1 receptor system.
  • To create novel PYR1-based biosensors with high sensitivity to specific ligands.
  • To demonstrate the application of these biosensors for detecting banned organophosphate contaminants and building genetic circuits.

Main Methods:

  • Design of an orthogonal '*' CID module featuring a dimer interface salt bridge.
  • X-ray crystallography, biochemical assays, and in vivo analyses to confirm module orthogonality.
  • Construction and testing of PYR1*MANDI/HAB1* and PYR1*AZIN/HAB1* systems in Arabidopsis thaliana and Saccharomyces cerevisiae.

Main Results:

  • The orthogonal '*' module was successfully designed and validated.
  • Engineered PYR1*MANDI/HAB1* and PYR1*AZIN/HAB1* systems exhibited nanomolar ligand sensitivity.
  • Demonstrated sensitive detection of organophosphate contaminants and construction of multi-input/output genetic circuits in living organisms.

Conclusions:

  • The novel ligand-programmable CID modules significantly expand the capabilities of synthetic biology tools.
  • These advancements enable the development of new plant-based and microbe-based sensing modalities.
  • The developed system offers a versatile platform for multi-channel chemical sensing and genetic circuit construction.