FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions
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 fluorou...
| Main Authors: | , , , , , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2023-06-01
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| Series: | Nature Communications |
| Online Access: | https://doi.org/10.1038/s41467-023-39078-0 |
| _version_ | 1797806658310635520 |
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| author | Guochen Qin Menghuan Qu Bei Jia Wei Wang Zhuojun Luo Chun-Peng Song W. Andy Tao Pengcheng Wang |
| author_facet | Guochen Qin Menghuan Qu Bei Jia Wei Wang Zhuojun Luo Chun-Peng Song W. Andy Tao Pengcheng Wang |
| author_sort | Guochen Qin |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-03-13T06:10:37Z |
| format | Article |
| id | doaj.art-97d2f4dac53e4fe1a436495fd7553612 |
| institution | Directory Open Access Journal |
| issn | 2041-1723 |
| language | English |
| last_indexed | 2024-03-13T06:10:37Z |
| publishDate | 2023-06-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Nature Communications |
| spelling | doaj.art-97d2f4dac53e4fe1a436495fd75536122023-06-11T11:19:33ZengNature PortfolioNature Communications2041-17232023-06-0114111510.1038/s41467-023-39078-0FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functionsGuochen Qin0Menghuan Qu1Bei Jia2Wei Wang3Zhuojun Luo4Chun-Peng Song5W. Andy Tao6Pengcheng Wang7Shanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of SciencesShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of SciencesShanghai Center for Plant Stress Biology, CAS Center for Excellence in Molecular Plant Sciences, Chinese Academy of SciencesState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan UniversityDepartment of Biochemistry, Purdue UniversityState Key Laboratory of Crop Stress Adaptation and Improvement, School of Life Sciences, Henan UniversityDepartment of Biochemistry, Purdue UniversityInstitute of Advanced Biotechnology and School of Life Sciences, Southern University of Science and TechnologyAbstract 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.https://doi.org/10.1038/s41467-023-39078-0 |
| spellingShingle | Guochen Qin Menghuan Qu Bei Jia Wei Wang Zhuojun Luo Chun-Peng Song W. Andy Tao Pengcheng Wang FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions Nature Communications |
| title | FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions |
| title_full | FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions |
| title_fullStr | FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions |
| title_full_unstemmed | FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions |
| title_short | FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1 in regulating ER functions |
| title_sort | fat switch based quantitative s nitrosoproteomics reveals a key role of gsnor1 in regulating er functions |
| url | https://doi.org/10.1038/s41467-023-39078-0 |
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