Hee-Jung Kim and Sura Ha contributed equally to this work.
ROSics: Chemistry and proteomics of cysteine modifications in redox biology
Article first published online: 10 JUN 2014
© 2014 The Authors. Mass Spectrometry Reviews published by Wiley Periodicals Inc.
This is an open access article under the terms of the Creative Commons Attribution-NonCommercial-NoDerivs License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non-commercial and no modifications or adaptations are made.
Mass Spectrometry Reviews
How to Cite
Kim, H.-J., Ha, S., Lee, H. Y. and Lee, K.-J. (2014), ROSics: Chemistry and proteomics of cysteine modifications in redox biology. Mass Spectrom. Rev.. doi: 10.1002/mas.21430
- Article first published online: 10 JUN 2014
- Manuscript Accepted: 20 NOV 2013
- Manuscript Revised: 30 APR 2013
- Manuscript Received: 4 AUG 2012
- Global Research Lab Program. Grant Number: 2012K1A1A2045441
- Proteogenomics Research Program. Grant Number: 2012M3A9B9036680
- WCU Project. Grant Number: R31-2008-000-10010-0
- redox biology;
- reactive oxygen species (ROS);
- cysteine modification;
- cysteine reactivity;
- mass spectrometry;
- thiosulfonic acid
Post-translational modifications (PTMs) occurring in proteins determine their functions and regulations. Proteomic tools are available to identify PTMs and have proved invaluable to expanding the inventory of these tools of nature that hold the keys to biological processes. Cysteine (Cys), the least abundant (1–2%) of amino acid residues, are unique in that they play key roles in maintaining stability of protein structure, participating in active sites of enzymes, regulating protein function and binding to metals, among others. Cys residues are major targets of reactive oxygen species (ROS), which are important mediators and modulators of various biological processes. It is therefore necessary to identify the Cys-containing ROS target proteins, as well as the sites and species of their PTMs. Cutting edge proteomic tools which have helped identify the PTMs at reactive Cys residues, have also revealed that Cys residues are modified in numerous ways. These modifications include formation of disulfide, thiosulfinate and thiosulfonate, oxidation to sulfenic, sulfinic, sulfonic acids and thiosulfonic acid, transformation to dehydroalanine (DHA) and serine, palmitoylation and farnesylation, formation of chemical adducts with glutathione, 4-hydroxynonenal and 15-deoxy PGJ2, and various other chemicals. We present here, a review of relevant ROS biology, possible chemical reactions of Cys residues and details of the proteomic strategies employed for rapid, efficient and sensitive identification of diverse and novel PTMs involving reactive Cys residues of redox-sensitive proteins. We propose a new name, “ROSics,” for the science which describes the principles of mode of action of ROS at molecular levels. © 2014 The Authors. Mass Spectrometry Reviews published by Wiley Periodicals Inc.