Proteomic examination of Ralstonia eutropha in cellular responses to formic acid.

In this study, Ralstonia eutropha was used to elucidate protein changes in response to formic acid. Sixty-three differentially expressed proteins in relation to formic acid in R. eutropha were found with 1-D PAGE and nano-LC-MS/MS. Among the proteins with decreased expression, four were involved in the shikimate pathway and three proteins in the pyrimidine biosynthesis pathway. With the increased expression of proteins, a dramatic change occurred in the induction of ion transporters in relation to maintenance of the acid-base balance. A detoxification process of formic acid in the bacteria might be related to a membrane enzyme, formate hydrogenylase. Three proteins in polyhydroxyalkanoate synthesis were enhanced and five proteins in glutathione biosynthesis increased in response to formic acid. Three enzymes in mevalonate biosynthesis and heat shock proteins were also elevated in the cells. Therefore, formic acid might have an inhibitory effect on aromatic amino acid production and pyrimidine biosynthesis in R. eutropha. R. eutropha cells seemed to attempt to overcome the effects of formic acid by increasing ion transporters and proteins that metabolized formic acid.