Identification of ENO2-targeted downstream genes by ChIP-seq in Arabidopsis
Ontology highlight
ABSTRACT:
ORGANISM(S): Arabidopsis thaliana
PROVIDER: GSE151305 | GEO | 2022/06/04
REPOSITORIES: GEO
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Project description:Hydrogen cyanide (HCN) is co-produced with ethylene in plant cell and enzymatically detoxified mainly by the mitochondrial ß-cyanoalanine synthase (CAS-C1). Permanent or transient depletion of CAS-C1 activity in Arabidopsis results in physiological alteration in the plant that point to the function of HCN as a gasotransmitter molecule. Label-free quantitative proteomic analysis of enriched mitochondrial samples isolated from wild type and cas-c1 mutant reveled significant changes in protein content, identifying 451 proteins that are absent or less abundant in cas-c1 and 353 proteins only present or more abundant in the mutant background. Gene onthology classification of these proteins highlights proteomic changes that explains the root hairless phenotype and the altered inmune response observed in cas-c1 mutant. The mechanism of action of cyanide as signaling molecule has been addressed by two proteomic approaches focused on identifying S-cyanylation of cysteine as a posttranslational modification of proteins. Both the 2-imino-thiazolidine chemical method and direct untargeted analysis of proteins by LC-MS/MS identified a set of 163 proteins susceptibles to be S-cyanylated that include sedoheptulose 1, 7 biphosphatase (SBPase), the peptidyl-prolyl cis-trans isomerase (CYP20-3) and enolase 2 (ENO2). In vitro analysis of these proteins identified this modification in SBPase Cys74, CYP20-3 Cys259 and ENO2 Cys346 residues that affected the enzymatic activity of the enzymes. GO classification and protein-protein interaction cluster analysis revealed the function of S-cyanylation in the regulation of primary metabolic pathways as glycolysis, and the Calvin and S-adenosylmethionine cicles.
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