Dataset Information

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 developed a highly sensitive and efficient fluorous affinity tag-switch (FAT-switch) chemical proteomics approach for S-nitrosylation peptide enrichment and detection. We quantitatively compared the global S-nitrosylation profiles in wild-type Arabidopsis and gsnor1/hot5/par2 mutant using this approach, and identifyied 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 revealed that S-nitrosylation at Cys337 in ER OXIDOREDUCTASE 1 (ERO1) causes the rearrangement of disulfide, resulting in enhanced ERO1 activity. This study offersed a powerful and applicable tool for S-nitrosylation research, which provides valuable resources for studies on S-nitrosylation-regulated ER functions in plants.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Whole Body

SUBMITTER: guochen qin

LAB HEAD: Pengcheng Wang

PROVIDER: PXD037504 | Pride | 2023-06-07

REPOSITORIES: Pride

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Dataset's files

Source:

			Action	DRS
	20190330_QGC_TFIA_C18_nGF_TMT.pdResult	Other
	20190330_QGC_TFIA_C18_nGF_TMT.raw	Raw
	20190504_G_1_210.pdResult	Other
	20190504_G_1_210.raw	Raw
	20190504_wt_1_210.raw	Raw

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Project description:Toxoplasma gondii transmitted via various route and rapidly duplicated during the acute infection, which caused the important zoonosis regarding to medicine and veterinary, toxoplasmosis. T. gondii possessed innate capability of producing nitric oxide (NO) and nitric oxide derivatives and S-nitrosylation not only participated in their signaling transduction, but also was a regulatory mechanism of protein post-translation. To date, S-nitrosylation proteome of T .gondii remains a mystery. In present study, we reported the first S-nitrosylated proteomic profile in T. gondii using mass spectrometry in combination with resin-assisted enrichment. 637 proteins were found to be S-nitrosylated and more than half of these S-nitrosylated proteins were localized in nucleus or cy-toplasm. Motif analysis identified seven motifs including five motifs containing lysine and two motif harboring isoleucine. GO enrichment revealed that S-nitrosylated proteins were mainly lo-cated in the mitochondrial inner membrane and organelle inner membrane in the cell. Those S-nitrosylated proteins were related with diverse biological and metabolic processes including or-ganic acid binding, carboxylic acid binding ribose and phosphate biosynthetic process. Glycoly-sis/gluconeogenesis and aminoacyl-tRNA biosynthesis were two remarkable pathways in which T. gondii S-nitrosylated proteins engaged. Twenty seven ribosomal proteins and eleven microneme proteins out of 22 secretory proteins were identified as S-nitrosylated proteins, which suggested that proteins in ribosome and microneme were S-nitrosylated with high proportion. PPI analysis identified three subnetworks with high relevancy ribosome, RNA transport and chaperonin com-plex component. These results implied that S-nitrosylated proteins in T. gondii were associated with protein translation in ribosome, gene transcription, invasion and proliferation of T. gondii. Our research firstly identified the S-nitrosylated proteomic profile of T. gondii and will provide a valuable resource for deep-going investigation of the functions of S-nitrosylation in T. gondii.

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

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