A biomimetic electrostatic assistance for guiding and promoting N-terminal protein chemical modification

Nathalie Ollivier, Magalie Sénéchal, Rémi Desmet, Benoît Snella, Vangelis Agouridas and Oleg Melnyk ()
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Nathalie Ollivier: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
Magalie Sénéchal: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
Rémi Desmet: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
Benoît Snella: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
Vangelis Agouridas: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille
Oleg Melnyk: Univ. Lille, CNRS, Inserm, CHU Lille, Institut Pasteur de Lille, U1019 - UMR 9017; Center for Infection and Immunity of Lille

Nature Communications, 2022, vol. 13, issue 1, 1-10

Abstract: Abstract The modification of protein electrostatics by phosphorylation is a mechanism used by cells to promote the association of proteins with other biomolecules. In this work, we show that introducing negatively charged phosphoserines in a reactant is a powerful means for directing and accelerating the chemical modification of proteins equipped with oppositely charged arginines. While the extra charged amino acid residues induce no detectable affinity between the reactants, they bring site-selectivity to a reaction that is otherwise devoid of such a property. They also enable rate accelerations of four orders of magnitude in some cases, thereby permitting chemical processes to proceed at the protein level in the low micromolar range, using reactions that are normally too slow to be useful in such dilute conditions.

Date: 2022
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DOI: 10.1038/s41467-022-34392-5

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