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• W2925654380 abstract "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." @default.
• W2925654380 created "2019-04-11" @default.
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• W2925654380 date "2019-05-08" @default.
• W2925654380 modified "2023-10-16" @default.
• W2925654380 title "Direct Zinc Finger Protein Persulfidation by H ₂ S Is Facilitated by Zn ²⁺" @default.
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• W2925654380 doi "https://doi.org/10.1002/anie.201900823" @default.
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