The interplay of Hfq, poly(A) polymerase I and exoribonucleases at the 3′ ends of RNAs resulting from Rho-independent termination

Régnier, Philippe; Hajnsdorf, Eliane

doi:10.4161/rna.23664

Cited by 26 publications

(26 citation statements)

References 116 publications

(243 reference statements)

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“…Strikingly, we found that the reduced levels of the 70S ribosomes in Hfq-depleted cells is dependent on residues located at the distal face of Hfq but not on those in the proximal and rim RNA-binding faces suggesting that rRNA regulation is independent of sRNA binding of Hfq. Namely, Hfq stimulates the addition of poly(A) tails to the 3 0 end of mRNAs containing Rho-independent transcription terminators, promoting their degradation in E. coli (Le Derout et al, 2003;Mohanty et al, 2004;Folichon et al, 2005;Régnier & Hajnsdorf, 2013). Hfq is known to act independently of an sRNA as partner in a variety of cellular functions.…”

Section: Discussionmentioning

confidence: 99%

The RNA ‐binding protein Hfq is important for ribosome biogenesis and affects translation fidelity

et al. 2018

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Ribosome biogenesis is a complex process involving multiple factors. Here, we show that the widely conserved RNA chaperone Hfq, which can regulate sRNA-mRNA basepairing, plays a critical role in rRNA processing and ribosome assembly in Hfq binds the 17S rRNA precursor and facilitates its correct processing and folding to mature 16S rRNA Hfq assists ribosome assembly and associates with pre-30S particles but not with mature 30S subunits. Inactivation of Hfq strikingly decreases the pool of mature 70S ribosomes. The reduction in ribosome levels depends on residues located in the distal face of Hfq but not on residues found in the proximal and rim surfaces which govern interactions with the sRNAs. Our results indicate that Hfq-mediated regulation of ribosomes is independent of its function as sRNA-regulator. Furthermore, we observed that inactivation of Hfq compromises translation efficiency and fidelity, both features of aberrantly assembled ribosomes. Our work expands the functions of the Sm-like protein Hfq beyond its function in small RNA-mediated regulation and unveils a novel role of Hfq as crucial in ribosome biogenesis and translation.

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Section: Discussionmentioning

confidence: 99%

The RNA ‐binding protein Hfq is important for ribosome biogenesis and affects translation fidelity

et al. 2018

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“…Hfq can stabilize RNAs, promote rapid RNAeRNA annealing, and unfold RNA regions (Sauer, 2013). It has additional roles (Regnier & Hajnsdorf, 2013;Sobrero & Valverde, 2012) and interacts with many proteins (Butland et al, 2005). Its particular function to recruit RNase E to target mRNAs, in conjunction with sRNAs, has been addressed above (Section 5.1.7).…”

Section: Hfqda Key Player In Srna Controlmentioning

confidence: 95%

Small RNAs in Bacteria and Archaea

Wagner

Romby

2015

Advances in Genetics

454

245

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“…For example, it has long been known that Hfq stabilizes A-tracts and oligo-(A) tails, which likely happens via the distal surface and arguably in a cooperative manner 16 , 33 - 35 , 42 , 55 - 57 . Furthermore, the proximal binding site can protect the 3′-oligo-(U) ends of Rho-independent transcripts from the attack of PNPase, 50 and uridine-rich sequences that are present in the interior of both mRNAs and sRNAs and are protected from RNaseE probably because they interact with the additional RNA-binding surfaces of Hfq 16 , 34 , 51 . In particular, many sRNAs are strongly destabilized in the absence of Hfq 22 , 23 , 52 …”

Section: Multiple Roles Of Hfq In Riboregulationmentioning

confidence: 99%

RNA binding by Hfq and ring-forming (L)Sm proteins

Weichenrieder¹

2014

RNA Biology

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The eukaryotic Sm and the Sm-like (LSm) proteins form a large family that includes LSm proteins in archaea and the Hfq proteins in bacteria. Commonly referred to as the (L)Sm protein family, the various members play important roles in RNA processing, decay, and riboregulation. Particularly interesting from a structural point of view is their ability to assemble into doughnut-shaped rings, which allows them to bind preferentially the uridine-rich 3′-end of RNA oligonucleotides. With an emphasis on Hfq, this review compares the RNA-binding properties of the various (L)Sm rings that were recently co-crystallized with RNA substrates, and it discusses how these properties relate to physiological function.

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The interplay of Hfq, poly(A) polymerase I and exoribonucleases at the 3′ ends of RNAs resulting from Rho-independent termination

Cited by 26 publications

References 116 publications

The RNA ‐binding protein Hfq is important for ribosome biogenesis and affects translation fidelity

The RNA ‐binding protein Hfq is important for ribosome biogenesis and affects translation fidelity

Small RNAs in Bacteria and Archaea

RNA binding by Hfq and ring-forming (L)Sm proteins

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