# Carrot and stick: how RNase R contributes to function and destruction of the translation machinery

**Authors:** Helge Paternoga, Lyudmila Dimitrova-Paternoga

PMC · DOI: 10.1080/15476286.2025.2535846 · RNA Biology · 2025-07-29

## TL;DR

This paper reviews how the enzyme RNase R helps regulate and break down RNA components involved in protein translation in bacteria.

## Contribution

The paper highlights new structural insights into RNase R's role in RNA homeostasis and translation machinery regulation.

## Key findings

- RNase R regulates and degrades components of the bacterial translation machinery.
- Recent structural studies reveal new details about RNase R's enzymatic activities.
- The enzyme plays a key role in trans-translation system regulation.

## Abstract

RNA is fundamental for life, and its homoeostasis is a critical contributor to cellular growth and adaptation to stress. Key RNA species include messenger RNA (mRNA) and non-coding RNAs, such as transfer RNA (tRNA), or ribosomal RNA (rRNA), that are essential for ribosome formation and translation of the genetic code. Furthermore, various other non-coding RNAs are expressed at each growth stage. Given RNA’s abundance and its role in all cellular processes, RNases – enzymes responsible for RNA degradation and processing – are central to RNA metabolism. In this review, we discuss the pivotal contribution of the 3’ exonuclease RNase R to bacterial RNA homoeostasis. We focus on its functions in regulating and degrading components of the translation machinery, including the trans-translation system, and we take a look at recent structural studies that shed new light on the activities of this important enzyme.

## Full-text entities

- **Diseases:** cancer (MESH:D009369), CSD (MESH:C562576), autoimmune conditions (MESH:D001327)
- **Chemicals:** pyrophosphate (MESH:C107241), metal (MESH:D008670), water (MESH:D014867), 2'-O-ribose methylation (-), magnesium (MESH:D008274), aspartates (MESH:D001224), cytosine (MESH:D003596), tyrosines (MESH:D014443), ATP (MESH:D000255), K (MESH:D011188), nucleotide (MESH:D009711), alanine (MESH:D000409)
- **Species:** Staphylococcus aureus (species) [taxon 1280], Caulobacter vibrioides (species) [taxon 155892], Streptococcus pneumoniae (species) [taxon 1313], Homo sapiens (human, species) [taxon 9606], Deinococcus radiodurans (species) [taxon 1299], Arabidopsis thaliana (mouse-ear cress, species) [taxon 3702], Mycoplasmoides genitalium (species) [taxon 2097], Trypanosoma brucei (species) [taxon 5691], Staphylococcus epidermidis (species) [taxon 1282], Haloferax (genus) [taxon 2251], Haloferax volcanii (species) [taxon 2246], Saccharomyces cerevisiae (baker's yeast, species) [taxon 4932], aureus [taxon 46170], Escherichia coli (E. coli, species) [taxon 562], Bacillus subtilis (species) [taxon 1423], Pseudomonas syringae (species) [taxon 317]
- **Mutations:** lysine-arginine

## Full text

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## Figures

8 figures with captions in the complete paper: https://tomesphere.com/paper/PMC12320835/full.md

## References

160 references — full list in the complete paper: https://tomesphere.com/paper/PMC12320835/full.md

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Source: https://tomesphere.com/paper/PMC12320835