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

Guochen Qin, Menghuan Qu, Bei Jia, Wei Wang, Zhuojun Luo, Chun-Peng Song, W. Andy Tao and Pengcheng Wang ()
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Guochen Qin: Chinese Academy of Sciences
Menghuan Qu: 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
Pengcheng Wang: Southern University of Science and Technology

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: 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.

Date: 2023
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DOI: 10.1038/s41467-023-39078-0

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