Direct Zinc Finger Protein Persulfidation by H2S Is Facilitated by Zn2+

Lange M, Ok K, Shimberg GD, Bursac B, Markó L, Ivanovic-Burmazovic I, Michel SL, Filipovic M (2019)


Publication Type: Journal article

Publication year: 2019

Journal

DOI: 10.1002/anie.201900823

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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APA:

Lange, M., Ok, K., Shimberg, G.D., Bursac, B., Markó, L., Ivanovic-Burmazovic, I.,... Filipovic, M. (2019). Direct Zinc Finger Protein Persulfidation by H2S Is Facilitated by Zn2+. Angewandte Chemie International Edition. https://dx.doi.org/10.1002/anie.201900823

MLA:

Lange, Mike, et al. "Direct Zinc Finger Protein Persulfidation by H2S Is Facilitated by Zn2+." Angewandte Chemie International Edition (2019).

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