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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, that 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.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Helicobacter Pylori B8

SUBMITTER: Thibaut Douché

LAB HEAD: Hilde De Reuse

PROVIDER: PXD023837 | Pride | 2021-04-08

REPOSITORIES: Pride

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			Action	DRS
	20190624-Helicobacter_pilory_693745.fasta	Fasta
	20200723_Q2_TD_ColQ2-78_Tejada_IP_B128-1.raw	Raw
	20200723_Q2_TD_ColQ2-78_Tejada_IP_B128-2.raw	Raw
	20200723_Q2_TD_ColQ2-78_Tejada_IP_B128-3.raw	Raw
	20200723_Q2_TD_ColQ2-78_Tejada_IP_B128-5.raw	Raw

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Similar Datasets

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

Project description:Ribonucleases (RNases) are central actors in post-transcriptional regulation, a major level of regulation of gene expression in all cells. This control plays an important role in the bacterial pathogen Helicobacter pylori, although only the function of RNase J was characterized so far. Here, we studied the RNase R enzyme from H. pylori, a 3’-5’ exoribonuclease whose ortholog in Escherichia coli was reported to display, in addition, helicase activity and to be able to hydrolyze RNA substrates with double stranded structures. We observed that HpRNase R protein does not carry the domains responsible for helicase activity in E. coli and accordingly that the purified protein is unable to degrade in vitro RNA molecules with secondary structures. The RNase R helicase domain loss is widespread among the Campylobacterota and occurred gradually during their evolution. Furthermore, an in vivo interaction between HpRNase R and RhpA, the sole DEAD-box RNA helicase of H. pylori, was discovered. Phylogenomics suggests that this interaction might occur in other bacteria of the phylum Campylobacterota. Purified RhpA facilitates the degradation of double stranded RNA substrates by HpRNase R, showing that this complex is functional. HpRNase R has a minor role of in 5S rRNA maturation and, as shown by RNA-Seq, few targets in H. pylori all of them being included in the RhpA regulon. In conclusion, we describe a new type of RNase R that lacks some of the features that were considered as hallmarks of RNase R proteins, but that has co-opted another RNA helicase, which we hypothesize helps it accomplish some of its functions in vivo.

2021-06-19 | E-MTAB-10045 | biostudies-arrayexpress

Acetylation regulates the oligomerization state and activity of RNase J, the major ribonuclease of Helicobacter pylori

Project description:In Helicobacter pylori, the major actor in post-transcriptional regulation is an RNA degradosome assembly composed of the essential ribonuclease RNase J and the DEAD-box RNA helicase RhpA. Here, we describe the oligomeric state and post-translational modifications of this protein complex. Our crystal structure of RNase J at 2.75 Å resolution reveals a homotetrameric quaternary state, and solution studies show that purified RNase J forms monomers and dimers, that RhpA is a monomer, and that the two proteins interact to form a stable complex with a 1:1 stoichiometry. Using mass spectrometry, we observed that RNase J is acetylated on multiple residues, one of which, K649, is important for RNase J oligomerization. Mutations targeting this residue and others affect the dimerization and in vitro activity of RNase J, suggesting that the dimer is the active form. In H. pylori, we observed that several of the identified acetylated residues impact on cell morphology, suggesting their importance for RNase J cellular function. Using H. pylori mutants, we found that several pathways contribute to RNase J acetylation. We propose acetylation as a regulatory level controlling RNase J properties and as a consequence the activity of the H. pylori RNA degradosome.

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HELZ2: a new, interferon-regulated, human 3’-5’ exoribonuclease of the RNB family is expressed from a non-canonical initiation codon

Project description:Proteins containing a RNB domain, originally identified in E. coli RNase II, are widely present throughout the tree of life. Many RNB proteins are endowed with 3’-5’ exoribonucleolytic activity but some have lost catalytic function during evolution. Database searches identified a new RNB domain containing protein in human: HELZ2. Analysis of genomic and expression data with evolutionary information suggested that the human HELZ2 protein is produced from an unforeseen non-canonical initiation codon in Hominidae. This unusual property was confirmed experimentally, extending the human protein by 247 residues. Human HELZ2 was further shown to be an active ribonuclease despite the substitution of a key residue in its catalytic center. HELZ2 harbors also two RNA helicase domains and several zinc-fingers and its expression is induced by interferon treatment. We demonstrate that HELZ2 is able to degrade structured RNAs through the coordinated ATP-dependent displacement of duplex RNA mediated by its RNA helicase domains and its 3’-5’ ribonucleolytic action. The expression characteristics and biochemical properties of HELZ2 support a role for this factor in response to viruses and/or mobile elements.

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Project description:Helicobacter pylori (H.pylori) infection is an important factor in the occurrence of human gastric diseases, but its pathogenic mechanism is not clear. N6-methyladenosine (m6A) is the most prevalent reversible methylation modification in mammalian RNA and it plays a crucial role in controlling many biological processes. We used MeRIP-seq technology to sequence the GES-1 cells infected with Helicobacter pylori(H. pylori) for 48 h.

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Expression data from AGS cells with Helicobacter pylori infection

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2024-04-18 | GSE264263 | GEO

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

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

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Transcription profiling of cell lines in response to Helicobacter pylori lipopolysaccharide shows Tribbles 3 - a novel regulator of TLR2-mediated signaling in response to Helicobacter pylori lipopolysaccharide

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