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

Journal article

Publication Details

Author(s): Lange M, Ok K, Shimberg GD, Bursac B, Markó L, Ivanovic-Burmazovic I, Michel SL, Filipovic M
Journal: Angewandte Chemie International Edition
Publication year: 2019
ISSN: 1433-7851
eISSN: 1521-3773


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

FAU Authors / FAU Editors

Filipovic, Milos
Lehrstuhl für Bioanorganische Chemie
Ivanovic-Burmazovic, Ivana Prof. Dr.
Lehrstuhl für Bioanorganische Chemie

External institutions with authors

Max-Delbrück-Centrum für Molekulare Medizin (MDC) Berlin-Buch
Université de Bordeaux
University of Maryland School of Pharmacy

How to cite

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.

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


Last updated on 2019-29-05 at 14:08