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Expression, Solubilization, and Purification of Eukaryotic Borate Transporters
Published on: March 7, 2019
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Post-translational insertion of boron in proteins to probe and modulate function
Tim A Mollner1, Patrick G Isenegger1, Brian Josephson1
1Department of Chemistry, Chemistry Research Laboratory, University of Oxford, Oxford, UK.
Nature Chemical Biology
|November 2, 2021
Summary
Researchers introduce boronoalanine (Bal), a novel boron-containing amino acid, into proteins. This enables new biological functions like enhanced stability and structure determination through unique boron bonding.
Area of Science:
- Biochemistry
- Bioinorganic Chemistry
- Protein Engineering
Background:
- Boron, an essential micronutrient, is typically absent in proteins.
- Boron's unique bonding properties offer potential for expanding biological functions beyond typical elements.
- Existing biological systems lack Lewis acidity modes available to boron.
Purpose of the Study:
- To demonstrate the site-selective incorporation of boron into proteins via a novel amino acid residue.
- To explore the functional capabilities of boron within protein structures, including Lewis acid-base pairing.
- To investigate how boron insertion impacts protein stability, structure, and reactivity.
Main Methods:
- Post-translational Cβ-Bγ bond formation for creating boronoalanine (Bal) residues.
- Site-selective anchoring of boron within complex biomolecular systems.
- Analysis of dative bond-mediated protein Lewis acid-base-pairing (LABP) interactions.
- Characterization of boron-mediated changes in protein stability and structure.
Main Results:
- Successful generation of boronoalanine (Bal) in proteins through mild, site-selective Cβ-Bγ bond formation.
- Demonstration of dative bond-mediated, site-dependent protein Lewis acid-base-pairing (LABP) by Bal.
- Observation of tunable inter- and intramolecular interactions and reactive sites via protein-LABP.
- Evidence of de novo functions including modulated thermo- and proteolytic stability and observation of transient structures.
Conclusions:
- Controlled boron insertion into proteins via Bal facilitates novel functionalities.
- Boron's unique chemistry enables stability modulation, structure determination, and de novo binding activities.
- Boron-modified proteins offer potential for redox-responsive modifications and advanced biomolecular engineering.
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