Journal article
Post-translational insertion of boron in proteins to probe and modulate function
- Abstract:
- Boron is absent in proteins, yet is a micronutrient. It possesses unique bonding that could expand biological function including modes of Lewis acidity not available to typical elements of life. Here we show that post-translational Cβ–Bγ bond formation provides mild, direct, site-selective access to the minimally sized residue boronoalanine (Bal) in proteins. Precise anchoring of boron within complex biomolecular systems allows dative bond-mediated, site-dependent protein Lewis acid–base-pairing (LABP) by Bal. Dynamic protein-LABP creates tunable inter- and intramolecular ligand–host interactions, while reactive protein-LABP reveals reactively accessible sites through migratory boron-to-oxygen Cβ–Oγ covalent bond formation. These modes of dative bonding can also generate de novo function, such as control of thermo- and proteolytic stability in a target protein, or observation of transient structural features via chemical exchange. These results indicate that controlled insertion of boron facilitates stability modulation, structure determination, de novo binding activities and redox-responsive ‘mutation’.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 8.8MB, Terms of use)
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(Preview, Corrected version of record, pdf, 676.6KB, Terms of use)
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- Publisher copy:
- 10.1038/s41589-021-00883-7
Authors
- Publisher:
- Springer Nature
- Journal:
- Nature Chemical Biology More from this journal
- Volume:
- 17
- Issue:
- 12
- Pages:
- 1245-1261
- Place of publication:
- United States
- Publication date:
- 2021-11-01
- Acceptance date:
- 2021-08-25
- DOI:
- EISSN:
-
1552-4469
- ISSN:
-
1552-4450
- Pmid:
-
34725511
- Language:
-
English
- Keywords:
- Pubs id:
-
1207857
- Local pid:
-
pubs:1207857
- Deposit date:
-
2021-11-19
- ARK identifier:
Terms of use
- Copyright holder:
- Mollner et al
- Copyright date:
- 2021
- Rights statement:
- © The Author(s) 2021. Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
- Notes:
- A correction to this article is available online from Springer Nature at: https://doi.org/10.1038/s41589-021-00957-6
- Licence:
- CC Attribution (CC BY)
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