Biochemical and structural characterization of the RlaP family nucleotidyltransferase potentially involved in RNA repair.

ABSTRACT: Nucleotidyltransferases (NTases) of Polβsuperfamily are highly diverse and play many important biological functions. However, many families of NTases remain uncharacterized. Because of physical proximity of the genes encoding NTases of PF10127 family to those encoding RNA ligases involved in RNA repair, PF10127 family of NTases was named RlaP (RNA ligase-associating Polβ). Here we report comprehensive characterization of two RlaP from Pseudomonas fluorescens and Pseudomonas aeruginosa (PfRlaP and PaRlaP), respectively. Our study showed that, among macromolecules isolated from E. coli cells, only RNAs are the substrates of RlaP. In vitro assays employing synthetic RNAs as substrates demonstrated that RlaP catalyzes addition of one or two nucleotide

SUBMITTER: Carruthers A 

PROVIDER: S-EPMC12776372 | biostudies-literature | 2025 Dec

REPOSITORIES: biostudies-literature