Reactive oxygen intermediates (ROIs) and reactive nitrogen intermediates (RNIs) have now become well established as important signalling molecules in physiological settings within microorganisms, mammals and plants. These intermediates are routinely synthesised in a highly controlled and transient fashion by NADPH-dependent enzymes, which constitute key regulators of redox signalling. Mild oxidants such as hydrogen peroxide (H2O2) and especially nitric oxide (NO) signal through chemical reactions with specific atoms of target proteins that result in covalent protein modifications. Specifically, highly reactive cysteine (Cys) residues of low pKa are a major site of action for these intermediates. The oxidation of target Cys residues can result in a number of distinct redox-based, post-translational modifications including S-nitrosylation, S-glutathionylation; and sulphenic acid, sulphinic acid and disulphide formation. Importantly, such modifications precisely regulate protein structure and function. Cys-based redox switches are now increasingly being found to underpin many different signalling systems and regulate physiological outputs across kingdoms.

The redox switch: dynamic regulation of protein function by cysteine modifications.

SPADARO, Davide Carmelo;
2010-01-01

Abstract

Reactive oxygen intermediates (ROIs) and reactive nitrogen intermediates (RNIs) have now become well established as important signalling molecules in physiological settings within microorganisms, mammals and plants. These intermediates are routinely synthesised in a highly controlled and transient fashion by NADPH-dependent enzymes, which constitute key regulators of redox signalling. Mild oxidants such as hydrogen peroxide (H2O2) and especially nitric oxide (NO) signal through chemical reactions with specific atoms of target proteins that result in covalent protein modifications. Specifically, highly reactive cysteine (Cys) residues of low pKa are a major site of action for these intermediates. The oxidation of target Cys residues can result in a number of distinct redox-based, post-translational modifications including S-nitrosylation, S-glutathionylation; and sulphenic acid, sulphinic acid and disulphide formation. Importantly, such modifications precisely regulate protein structure and function. Cys-based redox switches are now increasingly being found to underpin many different signalling systems and regulate physiological outputs across kingdoms.
2010
138
360
371
Spadaro D.; Yun B.-W.; Spoel S.; Chu C.; Wang Y.; Loake G.J.
File in questo prodotto:
File Dimensione Formato  
15 - PhyPla1.pdf

Accesso riservato

Tipo di file: PDF EDITORIALE
Dimensione 549.44 kB
Formato Adobe PDF
549.44 kB Adobe PDF   Visualizza/Apri   Richiedi una copia
15 PhyPla - POSTPRINT.pdf

Accesso aperto

Tipo di file: POSTPRINT (VERSIONE FINALE DELL’AUTORE)
Dimensione 227.06 kB
Formato Adobe PDF
227.06 kB Adobe PDF Visualizza/Apri

I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.

Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/101812
Citazioni
  • ???jsp.display-item.citation.pmc??? ND
  • Scopus 174
  • ???jsp.display-item.citation.isi??? 151
social impact