Persulfidation

Persulfidation (also called sulfhydration) is a type of post-translational modification of proteins involving addition of a sulfur molecule onto a reactive thiol (-SH) group of a cysteine residue.[1] Persulfidation occurs in plants,[2] animals,[3] and throughout all kingdoms.[4] It is a redox mechanism that regulates diverse biological processes in hydrogen sulfide (H2S) signaling by regulating protein functions and/or subcellular localizations.[5][6]

The added sulfur atom (or atoms) are in a chain (R-S-SH, R-S-S-SH.[7] These sulfur chains are unstable and react readily, making identification and quantification difficult.

This modification can be reversed back into a thiol by exogenous chemical reducing agents such as dithiothreitol (DTT) or TCEP, biological reducing agents such as glutathione, and proteins such as thioredoxin or glutaredoxin.[8][9]

References

  1. ^ M.R. Filipovic, Persulfidation (S-sulfhydration) and H2S. Handbook of experimental pharmacology 230 (2015) 29-59
  2. ^ A. Aroca, A. Serna, C. Gotor, and L. Romero, C., S-sulfhydration: a cysteine posttranslational modification in plant systems. Plant Physiology 168 (2015) 334-342
  3. ^ .K. Mustafa, M.M. Gadalla, N. Sen, S. Kim, W. Mu, S.K. Gazi, R.K. Barrow, G. Yang, R. Wang, and S.H. Snyder, H2S Signals Through Protein S-Sulfhydration. Sci. Signal. 2 (2009) ra72
  4. ^ Zivanovic J, Kouroussis E, Kohl JB, Adhikari B, Bursac B, Schott-Roux S, Petrovic D, Miljkovic JL, Thomas-Lopez D, Jung Y, Miler M, Mitchell S, Milosevic V, Gomes JE, Benhar M, Gonzalez-Zorn B, Ivanovic-Burmazovic I, Torregrossa R, Mitchell JR, Whiteman M, Schwarz G, Snyder SH, Paul BD, Carroll KS, Filipovic MR. Selective Persulfide Detection Reveals Evolutionarily Conserved Antiaging Effects of S-Sulfhydration. Cell Metab. 30(6), 1152-1170 (2019)
  5. ^ A. Aroca, C. Gotor, and L.C. Romero, Hydrogen Sulfide Signaling in Plants: Emerging Roles of Protein Persulfidation. Frontiers in plant science 9 (2018)
  6. ^ Filipovic MR, Zivanovic J, Alvarez B, Banerjee R. Chemical Biology of H(2)S Signaling through Persulfidation. Chem Rev. 118(3), 1253-1337 (2018)
  7. ^ Yang, Chun-tao; Devarie-Baez, Nelmi O.; Hamsath, Akil; Fu, Xiao-Dong; Xian, Ming (2020). "S-Persulfidation: Chemistry, Chemical Biology, and Significance in Health and Disease". Antioxidants & Redox Signaling. 33 (15): 1092–1114. doi:10.1089/ars.2019.7889. PMC 7583347. PMID 31547682.
  8. ^ Wedmann R, Onderka C, Wei S, Szijártó IA, Miljkovic JL, Mitrovic A, Lange M, Savitsky S, Yadav PK, Torregrossa R, Harrer EG, Harrer T, Ishii I, Gollasch M, Wood ME, Galardon E, Xian M, Whiteman M, Banerjee R, Filipovic MR. Improved tag-switch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation. Chem Sci. 7(5), 3414-3426 (2016)
  9. ^ É. Dóka, I. Pader, A. Bíró, K. Johansson, Q. Cheng, K. Ballagó, J.R. Prigge, D. Pastor-Flores, T.P. Dick, E.E. Schmidt, E.S.J. Arnér, and P. Nagy, A novel persulfide detection method reveals protein persulfide- and polysulfide-reducing functions of thioredoxin and glutathione systems. Science Advances 2 (2016)

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