RNase R is associated in a functional complex with the RhpA DEAD-box RNA helicase in Helicobacter pylori.

ABSTRACT: Ribonucleases are central players in post-transcriptional regulation, a major level of gene expression regulation in all cells. Here, we characterized the 3'-5' exoribonuclease RNase R from the bacterial pathogen Helicobacter pylori. The 'prototypical' Escherichia coli RNase R displays both exoribonuclease and helicase activities, but whether this latter RNA unwinding function is a general feature of bacterial RNase R had not been addressed. We observed that H. pylori HpRNase R protein does not carry the domains responsible for helicase activity and accordingly the purified protein is unable to degrade in vitro RNA molecules with secondary structures. The lack of RNase R helicase domains is widespread among the Campylobacterota, which include Helicobacter and Campylobacter genera, and this

SUBMITTER: Tejada-Arranz A 

PROVIDER: S-EPMC8136821 | biostudies-literature | 2021 May

REPOSITORIES: biostudies-literature