Direct Zinc Finger Protein Persulfidation by H2 S Is Facilitated by Zn2.
Angew Chem Int Ed Engl
; 58(24): 7997-8001, 2019 06 11.
Article
em En
| MEDLINE
| ID: mdl-30924279
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Zinco
/
Dedos de Zinco
/
Tristetraprolina
/
Sulfeto de Hidrogênio
Limite:
Animals
Idioma:
En
Revista:
Angew Chem Int Ed Engl
Ano de publicação:
2019
Tipo de documento:
Article
País de afiliação:
Alemanha