The cysteine proteome

We address the redox regulation systems, especially focusing on major reducing systems that balance the oxidative reactions and support a rapidly evolving understanding of the spatiotemporal nature of redox regulation

Young-Mi Go; Joshua D. Chandler; Dean P. Jones


Scholarcy highlights

  • The sulfur atom of cysteine provides a considerable range of chemical reactivity and structural flexibility in the proteome
  • These often share related oxidative phenotypes and mechanisms, and progress in redox systems biology is beginning to provide an understanding of the integration of the underlying redox systems
  • Studies in yeast showed that the redox proteome was preserved in cells deficient in the GSH system but not in cells with compromised Trx systems. These results show that the Trx system is most central in regulation of the yeast Cys proteome
  • The dynamic nature and functional importance of compartment-specific control of the Cys proteome are further illustrated by Trx-dependent protection against cellular stresses associated with growth inhibition and cell death induced by H2O2, TNF╬▒ and chemotherapeutic agents
  • S-nitrosylation represents a series of modifications of the Cys proteome, which can be considered parallel to the oxidative systems in providing a network of regulatory elements impacting diverse aspects of cell function
  • Comparison of sulfenylated Cys residues in 193 proteins with previously identified targets of glutathionylation, disulfide formation and S-nitrosylation shows minimal overlap. These results suggest that different Cys modifications are selectively targeted toward different subsets of the Cys proteome rather than serving as multidirectional switches

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