H2S directly modifies the zinc finger protein TTP via persulfidation, inhibiting its mRNA binding function, which may have implications for TNFα regulation.
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H₂ S is a gaseous signaling molecule that modifies cysteine residues in proteins to form persulfides (P-SSH). One family of proteins modified by H₂ S are zinc finger (ZF) proteins, which contain multiple zinc-coordinating cysteine residues. Herein, we report the reactivity of H₂ S with a ZF protein called tristetraprolin (TTP). Rapid persulfidation leading to complete thiol oxidation of TTP mediated by H₂ S was observed by low-temperature ESI-MS and fluorescence spectroscopy. Persulfidation of TTP required O₂ , which reacts with H₂ S to form superoxide, as detected by ESI-MS, a hydroethidine fluorescence assay, and EPR spin trapping. H₂ S was observed to inhibit TTP function (binding to TNFα mRNA) by an in vitro fluorescence anisotropy assay and to modulate TNFα in vivo. H₂ S was unreactive towards TTP when the protein was bound to RNA, thus suggesting a protective effect of RNA.
Hypothesis-generating for H2S in TNFα regulation; leaves open human translational relevance.
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Lange et al. (2019) studied this question.
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