We applied an iodoacetyl tandem mass tags (iodoTMT)-based proteomic approach to analyze the redox proteome of Brassica napus seedlings under control and salt-stressed conditions. We identified 1,821 sulfenylated sites in 912 proteins from all samples.

ABSTRACT: By means of large-scale redox proteomics, we studied reversible cysteine modification during the response to short-term salt stress in Brassica napus. We applied an iodoacetyl tandem mass tags (iodoTMT)-based proteomic approach to analyze the redox proteome of Brassica napus seedlings under control and salt-stressed conditions. We identified 1,821 sulfenylated sites in 912 proteins from all samples. A great number of sulfenylated proteins were predicted to localize to chloroplasts and cytoplasm and GO enrichment analysis of differentially sulfenylated proteins revealed that metabolic processes such as photosynthesis and glycolysis are enriched and enzymes are overrepresented. Redox-sensitive sites in two enzymes were validated in vitro on recombinant proteins and they might affect the enzyme activity. This targeted approach contributes to the identification of the sulfenylated sites and proteins in Brassica napus subjected to salt stress and our study will improve our understanding of the molecular mechanisms underlying the redox regulation in response to salt stress.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Brassica Napus (rape)

TISSUE(S): Plant Cell, Leaf

SUBMITTER: Liangqian Yu  

LAB HEAD: Liang Guo

PROVIDER: PXD027721 | Pride | 2021-08-18

REPOSITORIES: Pride