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

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.

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Publication Details

Journal
Agronomy
Published
2024-11-21
DOI
https://doi.org/10.3390/agronomy14122757
Citations
3
Primary Topic
Redox biology and oxidative stress
Type
article
Field-Weighted Citation Impact
0.70

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article

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

Yang‐Dong Guo, F‐M Chen, Na Zhang, Ying Liu et al.
3 citations
Agronomy
Redox biology and oxidative stress
0.70
article

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

Yang‐Dong Guo, F‐M Chen, Na Zhang, Ying Liu, Xiaoyun Wang, Hongxin Li, Bing Zhao, Peiyang Zhang
article en
3 citations

Abstract

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.

AgronomyVol. 14(12)
Beijing University of Agriculture (CN), China Agricultural University (CN)
China Agricultural University
Life in Land
Openalex Percentile: Top 29%
Redox biology and oxidative stress
0.70
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Cysteine Thiol-Based Oxidative Post-Translational Modifications Fine-Tune Protein Functions in Plants — Yang‐Dong Guo, F‐M Chen, et al. · Agronomy (2024) | TGRS Research Map | TGRS