Article Dans Une Revue Angewandte Chemie International Edition Année : 2019

Direct Zinc Finger Protein Persulfidation by H\textsubscript2 S Is Facilitated by Zn\textsuperscript2+

Résumé

Abstract H 2 S is a gaseous signaling molecule that modifies cysteine residues in proteins to form persulfides (P-SSH). One family of proteins modified by H 2 S are zinc finger (ZF) proteins, which contain multiple zinc-coordinating cysteine residues. Herein, we report the reactivity of H 2 S with a ZF protein called tristetraprolin (TTP). Rapid persulfidation leading to complete thiol oxidation of TTP mediated by H 2 S was observed by low-temperature ESI-MS and fluorescence spectroscopy. Persulfidation of TTP required O 2 \,, which reacts with H 2 S to form superoxide, as detected by ESI-MS, a hydroethidine fluorescence assay, and EPR spin trapping. H 2 S was observed to inhibit TTP function (binding to TNFα mRNA) by an in vitro fluorescence anisotropy assay and to modulate TNFα in vivo. H 2 S was unreactive towards TTP when the protein was bound to RNA, thus suggesting a protective effect of RNA.
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Dates et versions

hal-04833212 , version 1 (12-12-2024)

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Mike Lange, Kiwon Ok, Geoffrey D. Shimberg, Biljana Bursac, Lajos Markó, et al.. Direct Zinc Finger Protein Persulfidation by H\textsubscript2 S Is Facilitated by Zn\textsuperscript2+. Angewandte Chemie International Edition, 2019, 58 (24), pp.7997--8001. ⟨10.1002/anie.201900823⟩. ⟨hal-04833212⟩

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