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FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions

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  • Guochen Qin

    (Chinese Academy of Sciences
    Peking University Institute of Advanced Agricultural Sciences, Shandong Laboratory of Advanced Agricultural Sciences at Weifang)

  • Menghuan Qu

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Bei Jia

    (Chinese Academy of Sciences)

  • Wei Wang

    (Henan University)

  • Zhuojun Luo

    (Purdue University)

  • Chun-Peng Song

    (Henan University)

  • W. Andy Tao

    (Purdue University
    Purdue University)

  • Pengcheng Wang

    (Southern University of Science and Technology)

Abstract

Reversible protein S-nitrosylation regulates a wide range of biological functions and physiological activities in plants. However, it is challenging to quantitively determine the S-nitrosylation targets and dynamics in vivo. In this study, we develop a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compare the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identify 2,121 S-nitrosylation peptides in 1,595 protein groups, including many previously unrevealed S-nitrosylated proteins. These are 408 S-nitrosylated sites in 360 protein groups showing an accumulation in hot5-4 mutant when compared to wild type. Biochemical and genetic validation reveal that S-nitrosylation at Cys337 in ER OXIDOREDUCTASE 1 (ERO1) causes the rearrangement of disulfide, resulting in enhanced ERO1 activity. This study offers a powerful and applicable tool for S-nitrosylation research, which provides valuable resources for studies on S-nitrosylation-regulated ER functions in plants.

Suggested Citation

  • Guochen Qin & Menghuan Qu & Bei Jia & Wei Wang & Zhuojun Luo & Chun-Peng Song & W. Andy Tao & Pengcheng Wang, 2023. "FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-39078-0
    DOI: 10.1038/s41467-023-39078-0
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    References listed on IDEAS

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    1. Byung-Wook Yun & Angela Feechan & Minghui Yin & Noor B. B. Saidi & Thierry Le Bihan & Manda Yu & John W. Moore & Jeong-Gu Kang & Eunjung Kwon & Steven H. Spoel & Jacqueline A. Pallas & Gary J. Loake, 2011. "S-nitrosylation of NADPH oxidase regulates cell death in plant immunity," Nature, Nature, vol. 478(7368), pages 264-268, October.
    2. Ruzanna Mnatsakanyan & Stavroula Markoutsa & Kim Walbrunn & Andreas Roos & Steven H. L. Verhelst & René P. Zahedi, 2019. "Proteome-wide detection of S-nitrosylation targets and motifs using bioorthogonal cleavable-linker-based enrichment and switch technique," Nature Communications, Nature, vol. 10(1), pages 1-12, December.
    3. Jian Feng & Chun Wang & Qingguo Chen & Hui Chen & Bo Ren & Xiaoming Li & Jianru Zuo, 2013. "S-nitrosylation of phosphotransfer proteins represses cytokinin signaling," Nature Communications, Nature, vol. 4(1), pages 1-9, June.
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