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

Alejandro Tejada-Arranz, Rute G. Matos, Yves Quentin, Maxime Bouilloux-Lafont, Eloïse Galtier, Valérie Briolat, Etienne Kornobis, Thibaut Douché, Mariette Matondo, Cecilia M. Arraiano, Bertrand Raynal, Hilde De Reuse

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

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 loss occurred gradually during their evolution. An in vivo interaction between HpRNase R and RhpA, the sole DEAD-box RNA helicase of H. pylori was discovered. Purified RhpA facilitates the degradation of double stranded RNA by HpRNase R, showing that this complex is functional. HpRNase R has a minor role in 5S rRNA maturation and few targets in H. pylori, all included in the RhpA regulon. We concluded that during evolution, HpRNase R has co-opted the RhpA helicase to compensate for its lack of helicase activity.

Original languageEnglish
Pages (from-to)5249-5264
Number of pages16
JournalNucleic Acids Research
Volume49
Issue number9
DOIs
Publication statusPublished - 21 May 2021

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