Publication Information
Qin et al., 2023
Abstract
Nat Commun. 2023 Jun 5;14(1):3268. doi: 10.1038/s41467-023-39078-0.
FAT-switch-based quantitative S-nitrosoproteomics reveals a key role of GSNOR1
in regulating ER functions.
Qin G(1)(2), Qu M(1)(3), Jia B(1), Wang W(4), Luo Z(5), Song CP(4), Tao
WA(5)(6), Wang P(7).
Author information:
(1)Shanghai Center for Plant Stress Biology, CAS Center for Excellence in
Molecular Plant Sciences, Chinese Academy of Sciences, 200032, Shanghai, China.
(2)Peking University Institute of Advanced Agricultural Sciences, Shandong
Laboratory of Advanced Agricultural Sciences at Weifang, 261000, Weifang,
Shandong, China.
(3)University of Chinese Academy of Sciences, Beijing, China.
(4)State Key Laboratory of Crop Stress Adaptation and Improvement, School of
Life Sciences, Henan University, 475004, Kaifeng, China.
(5)Department of Biochemistry, Purdue University, West Lafayette, IN, 47907,
USA.
(6)Department of Chemistry, Purdue University, West Lafayette, IN, 47907, USA.
(7)Institute of Advanced Biotechnology and School of Life Sciences, Southern
University of Science and Technology, 518055, Shenzhen, China.
wangpc@sustech.edu.cn.
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.
© 2023. The Author(s).
DOI: 10.1038/s41467-023-39078-0
PMCID: PMC10241878
PMID: 37277371 [Indexed for MEDLINE]
Conflict of interest statement: The authors declare no competing interests.
