Data on intracellular localization of RPSA upon alteration of its redox state

Ribosomal Protein SA (RPSA), a component of the 40S ribosomal subunit, was identified as a H(2)O(2) target in HeLa cells [1]. In order to analyze the intracellular localization of RPSA in different redox states we overexpressed wild-type RPSA (RPSAwt) or RPSA containing two cysteine to serine residue substitutions at positions 148 and 163 (RPSAmut) in HeLa cells. The transfected cells were exposed to H(2)O(2) or N-acetylcysteine (NAC) and RPSA subcellular localization was assessed by immunofluorescence in permeabilized cells. In addition, co-immunofluorescence for RPSA and Ribosomal Protein S6 (RPS6) was performed in cells overexpressing RPSAwt or RPSAmut. Finally, the ribosomal expression of endogenous RPSA in the presence or absence of H(2)O(2) was analyzed by Western blot. The data presented in this work is related to the research article entitled “Hydrogen peroxide regulates cell adhesion through the redox sensor RPSA” [1].