Direct Zinc Finger Protein Persulfidation by H2 S Is Facilitated by Zn2
© 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2019 |
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| Erschienen: |
2019 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:58 |
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| Enthalten in: |
Angewandte Chemie (International ed. in English) - 58(2019), 24 vom: 11. Juni, Seite 7997-8001 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Lange, Mike [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 08.09.2020 Date Revised 08.09.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1002/anie.201900823 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM295464097 |
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| 520 | |a © 2019 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, N.I.H., Extramural | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Research Support, U.S. Gov't, Non-P.H.S. | |
| 650 | 4 | |a hydrogen sulfide | |
| 650 | 4 | |a mass spectrometry | |
| 650 | 4 | |a persulfidation | |
| 650 | 4 | |a superoxide | |
| 650 | 4 | |a zinc finger proteins | |
| 650 | 7 | |a Sulfides |2 NLM | |
| 650 | 7 | |a Tristetraprolin |2 NLM | |
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| 700 | 1 | |a Ok, Kiwon |e verfasserin |4 aut | |
| 700 | 1 | |a Shimberg, Geoffrey D |e verfasserin |4 aut | |
| 700 | 1 | |a Bursac, Biljana |e verfasserin |4 aut | |
| 700 | 1 | |a Markó, Lajos |e verfasserin |4 aut | |
| 700 | 1 | |a Ivanović-Burmazović, Ivana |e verfasserin |4 aut | |
| 700 | 1 | |a Michel, Sarah L J |e verfasserin |4 aut | |
| 700 | 1 | |a Filipovic, Milos R |e verfasserin |4 aut | |
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