Identification of 2-oxohistidine Interacting Proteins Using E. coli Proteome Chips.

ABSTRACT: Cellular proteins are constantly damaged by reactive oxygen species generated by cellular respiration. Because of its metal-chelating property, the histidine residue is easily oxidized in the presence of Cu/Fe ions and H₂O₂ via metal-catalyzed oxidation, usually converted to 2-oxohistidine. We hypothesized that cells may have evolved antioxidant defenses against the generation of 2-oxohistidine residues on proteins, and therefore there would be cellular proteins which specifically interact with this oxidized side chain. Using two chemically synthesized peptide probes containing 2-oxohistidine, high-throughput interactome screening was conducted using the E. coli K12 proteome microarray containing >4200 proteins. Ten interacting proteins were identified, and successful

SUBMITTER: Lin JM 

PROVIDER: S-EPMC5141273 | biostudies-literature | 2016 Dec

REPOSITORIES: biostudies-literature