Cysteine Thiol-Based Oxidative Post-Translational Modifications Fine-Tune Protein Functions in Plants

This is the authors' abstract. We don't add key points for this paper.

Post-translational modification is a prerequisite for the functions of intracellular proteins. Thiol-based oxidative post-translational modifications (OxiPTMs) mainly include S-sulfenylation, S-nitrosation, persulfidation, and S-glutathionylation. Reactive electrophilic species can reversibly or irreversibly oxidize redox-sensitive proteins, thereby exerting dual effects on plant growth, development, and environmental stress. Recent studies have shown that transcription factors (TFs) are main targets of OxiPTMs. The majority of TFs transmit redox signals by altering their transcriptional activity, while some non-transcription factors can also accept post-translational redox modifications. Here, we provide an overview of the known types of OxiPTMs, the reactive electrophilic species that induce OxiPTMs, and the significance of OxiPTMs in fine-tuning TF and non-TF proteins. This review will provide a more comprehensive understanding of the dynamic regulation of protein functions in response to stress.