Dinucleoside tetraphosphates have been shown to function in bacteria as precursors to nucleoside tetraphosphate (Np₄) RNA caps. The removal of this cap is critical for initiating 5′ end-dependent degradation of those RNAs, which affects bacterial adaptability to stress. This study described that the RNA pyrophosphohydrolase (RppH) assumes a leading role in decapping those transcripts in Escherichia coli (E. coli) cells under conditions of disulfide stress. This enzyme recognizes Np₄-capped 5′ ends by a mechanism distinct from the one it uses to recognize other 5′ termini, which generates a triphosphorylated RNA intermediate that must undergo further deprotection by RppH to trigger degradation.

The dataset contains atomic coordinates for the complex of RppH as well as supplementary data tied to the publication. The supplementary data contains three tables about first-order rate constants measured in E. coli, data collection and refinement statistics for the RppH-Ap₄A complex, and oligonucleotides used in the study. The study showed that the distinct manner in which RppH recognizes Np₄-capped 5′ ends and its differential impact on the rates at which such termini are deprotected could have major consequences for reprogramming gene expression during disulfide stress.