Protein S-nitrosylation in photosynthetic organisms: A comprehensive overview with future perspectives

•NO/RNS activity in vivo depends on biosynthesis, reactivity and scavenging systems.•NO is a radical, as such it chiefly reacts with other radicals and transition metals.•NO/RNS promote nitrosothiol formation in selected protein cysteines.•Nitrosylation vs. denitrosylation reactions set the levels of nitrosothiols in vivo.•Proteomic techniques show the pervasivity of protein nitrosylation in phototrophs.

BackgroundThe free radical nitric oxide (NO) and derivative reactive nitrogen species (RNS) play essential roles in cellular redox regulation mainly through protein S-nitrosylation, a redox post-translational modification in which specific cysteines are converted to nitrosothiols.Scope of viewThis review aims to discuss the current state of knowledge, as well as future perspectives, regarding protein S-nitrosylation in photosynthetic organisms.Major conclusionsNO, synthesized by plants from different sources (nitrite, arginine), provides directly or indirectly the nitroso moiety of nitrosothiols. Biosynthesis, reactivity and scavenging systems of NO/RNS, determine the NO-based signaling including the rate of protein nitrosylation. Denitrosylation reactions compete with nitrosylation in setting the levels of nitrosylated proteins in vivo.General significanceBased on a combination of proteomic, biochemical and genetic approaches, protein nitrosylation is emerging as a pervasive player in cell signaling networks. Specificity of protein nitrosylation and integration among different post-translational modifications are among the major challenges for future experimental studies in the redox biology field. This article is part of a Special Issue entitled: Plant Proteomics — a bridge between fundamental processes and crop production, edited by Dr. Hans-Peter Mock.