Airpnp: Auto- and Integrated Regulation of Polynucleotide Phosphorylase

Condon, Ciarán

doi:10.1128/jb.00794-15

Cited by 3 publications

(1 citation statement)

References 26 publications

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“…PNPase may play a chaperone role for some sRNAs [67][68][69][70]. The chaperone property opens the possibility that regulatory RNA recruitment by PNPase could modulate the activity of the degradosome.…”

Section: The Exosome-like Pnpasementioning

confidence: 99%

RNase E and the High-Fidelity Orchestration of RNA Metabolism

Bandyra

Luisi

2018

Microbiol Spectr

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The bacterial endoribonuclease RNase E occupies a pivotal position in the control of gene expression, as its actions either commit transcripts to an irreversible fate of rapid destruction or unveil their hidden functions through specific processing. Moreover, the enzyme contributes to quality control of rRNAs. The activity of RNase E can be directed and modulated by signals provided through regulatory RNAs that guide the enzyme to specific transcripts that are to be silenced. Early in its evolutionary history, RNase E acquired a natively unfolded appendage that recruits accessory proteins and RNA. These accessory factors facilitate the activity of RNase E and include helicases that remodel RNA and RNA-protein complexes, and polynucleotide phosphorylase, a relative of the archaeal and eukaryotic exosomes. RNase E also associates with enzymes from central metabolism, such as enolase and aconitase. RNase E-based complexes are diverse in composition, but generally bear mechanistic parallels with eukaryotic machinery involved in RNA-induced gene regulation and transcript quality control. That these similar processes arose independently underscores the universality of RNA-based regulation in life. Here we provide a synopsis and perspective of the contributions made by RNase E to sustain robust gene regulation with speed and accuracy.

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Section: The Exosome-like Pnpasementioning

confidence: 99%

RNase E and the High-Fidelity Orchestration of RNA Metabolism

Bandyra

Luisi

2018

Microbiol Spectr

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RNase E and the High-Fidelity Orchestration of RNA Metabolism

Bandyra

Luisi

2018

Regulating With RNA in Bacteria and Archaea

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The bacterial endoribonuclease RNase E occupies a pivotal position in the control of gene expression, as its actions either commit transcripts to an irreversible fate of rapid destruction or unveil their hidden functions through specific processing. Moreover, the enzyme contributes to quality control of ribosomal RNAs. The activity of RNase E can be directed and modulated by signals provided through regulatory RNAs that guide the enzyme to specific transcripts that are to be silenced. At a comparatively early stage of its evolutionary history, RNase E acquired a natively unfolded appendage that recruits accessory proteins and RNA. These accessory factors facilitate the activity of RNase E and include helicases that remodel RNA and RNAprotein complexes, and polynucleotide phosphorylase, a relative of the archaeal and eukaryotic exosomes. RNase E also associates with 2 enzymes from central metabolism, such as enolase and aconitase. RNase E-based complexes are diverse in composition, but generally bear mechanistic parallels with eukaryotic machinery involved in RNA-induced gene regulation and transcript quality control. That these similar processes arose independently underscores the universality of RNA-based regulation in life. A synopsis and perspective is provided of the contributions made by RNase E to sustain robust gene regulation with speed and accuracy. RNase E EC number 3.1.26.12

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Pseudomonas aeruginosa Polynucleotide Phosphorylase Controls Tolerance to Aminoglycoside Antibiotics by Regulating the MexXY Multidrug Efflux Pump

Fan

Pan

Wang

et al. 2021

Antimicrob Agents Chemother

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Pseudomonas aeruginosa is an opportunistic pathogen that shows high intrinsic resistance to a variety of antibiotics. The MexX-MexY-OprM efflux pump plays an important role in the bacterial resistance to aminoglycoside antibiotics. Polynucleotide phosphorylase (PNPase) is a highly conserved exonuclease that plays important roles in RNA processing and bacterial response to environmental stresses. Previously, we demonstrated that PNPase controls the tolerance to fluoroquinolone antibiotics by influencing the production of pyocin in P. aeruginosa. In this study, we found that mutation of the PNPase coding gene (pnp) in P. aeruginosa increases the bacterial tolerance to aminoglycoside antibiotics. We further demonstrate that upregulation of the mexXY genes is responsible for the increased tolerance in the pnp mutant. Furthermore, our experimental results revealed that PNPase controls translation of the armZ mRNA through its 5′ untranslated region (5′-UTR). ArmZ had previously been shown to positively regulate the expression of mexXY. Therefore, our results revealed a novel role of PNPase in the regulation of armZ and subsequently the MexXY efflux pump.

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Airpnp: Auto- and Integrated Regulation of Polynucleotide Phosphorylase

Cited by 3 publications

References 26 publications

RNase E and the High-Fidelity Orchestration of RNA Metabolism

RNase E and the High-Fidelity Orchestration of RNA Metabolism

RNase E and the High-Fidelity Orchestration of RNA Metabolism

Pseudomonas aeruginosa Polynucleotide Phosphorylase Controls Tolerance to Aminoglycoside Antibiotics by Regulating the MexXY Multidrug Efflux Pump

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