<scp>H</scp>fq binds directly to the ribosome‐binding site of <scp>IS</scp><i>10</i> transposase m<scp>RNA</scp> to inhibit translation

Ellis, Mary; Trussler, Ryan S.; Haniford, David B.

doi:10.1111/mmi.12961

Cited by 60 publications

(83 citation statements)

References 66 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The four sRNAs assigned to this group are dependent upon the proximal and distal sites for full accumulation. Our results are consistent with the results of others showing distal site interactions for RprA and OxyS (Updegrove et al, 2008;Olejniczak, 2011), both in the intermediate class of sRNAs in our tests, and distal face binding to A-rich sequences in ChiX (Ellis et al, 2015;Małecka et al, 2015). These results suggest a model in which Class II sRNAs bind to the proximal and distal sites (Fig 3).…”

Section: Discussionsupporting

confidence: 93%

Alternative Hfq‐sRNA interaction modes dictate alternative mRNA recognition

et al. 2015

View full text Add to dashboard Cite

Many bacteria use small RNAs (sRNAs) and the RNA chaperone Hfq to regulate mRNA stability and translation. Hfq, a ring-shaped homohexamer, has multiple faces that can bind both sRNAs and their mRNA targets. We find that Hfq has at least two distinct ways in which it interacts with sRNAs; these different binding properties have strong effects on the stability of the sRNA in vivo and the sequence requirements of regulated mRNAs. Class I sRNAs depend on proximal and rim Hfq sites for stability and turn over rapidly. Class II sRNAs are more stable and depend on the proximal and distal Hfq sites for stabilization. Using deletions and chimeras, we find that while Class I sRNAs regulate mRNA targets with previously defined ARN repeats, Class II sRNAs regulate mRNAs carrying UA-rich rim-binding sites. We discuss how these different binding modes may correlate with different roles in the cell, with Class I sRNAs acting as emergency responders and Class II sRNAs acting as silencers.

show abstract

Section: Discussionsupporting

confidence: 93%

Alternative Hfq‐sRNA interaction modes dictate alternative mRNA recognition

et al. 2015

View full text Add to dashboard Cite

show abstract

“…In another example, Hfq has been shown to compete with RyhB sRNA for binding to cirA mRNA, which leads to their opposite functions in the regulation (Salvail et al 2013). Finally, Hfq has been proposed to repress translation independently of sRNAs by direct binding to amiE mRNA (Sonnleitner and Blasi 2014) or to RNA-IN mRNA (Ellis et al 2015). Overall, these data indicate that Hfq may have different contributions to sRNA stability, their annealing to mRNAs, and translation regulation.…”

Section: Introductionmentioning

confidence: 81%

Hfq assists small RNAs in binding to the coding sequence of ompD mRNA and in rearranging its structure

Wróblewska

Olejniczak

2016

RNA

View full text Add to dashboard Cite

The bacterial protein Hfq participates in the regulation of translation by small noncoding RNAs (sRNAs). Several mechanisms have been proposed to explain the role of Hfq in the regulation by sRNAs binding to the 5 ′ -untranslated mRNA regions. However, it remains unknown how Hfq affects those sRNAs that target the coding sequence. Here, the contribution of Hfq to the annealing of three sRNAs, RybB, SdsR, and MicC, to the coding sequence of Salmonella ompD mRNA was investigated. Hfq bound to ompD mRNA with tight, subnanomolar affinity. Moreover, Hfq strongly accelerated the rates of annealing of RybB and MicC sRNAs to this mRNA, and it also had a small effect on the annealing of SdsR. The experiments using truncated RNAs revealed that the contributions of Hfq to the annealing of each sRNA were individually adjusted depending on the structures of interacting RNAs. In agreement with that, the mRNA structure probing revealed different structural contexts of each sRNA binding site. Additionally, the annealing of RybB and MicC sRNAs induced specific conformational changes in ompD mRNA consistent with local unfolding of mRNA secondary structure. Finally, the mutation analysis showed that the long AU-rich sequence in the 5 ′ -untranslated mRNA region served as an Hfq binding site essential for the annealing of sRNAs to the coding sequence. Overall, the data showed that the functional specificity of Hfq in the annealing of each sRNA to the ompD mRNA coding sequence was determined by the sequence and structure of the interacting RNAs.

show abstract

“…Despite Hfq being widely conserved, Hfq-dependent regulation of sRNAs is not a common feature; for example, this function is missing in many bacteria like Bacillus subtilis and Listeria monocytogenes (Christiansen et al, 2006;Rochat et al, 2015). Also, Hfq inhibits translation by binding directly to mRNAs, independent of a sRNA partner (Salvail et al, 2013;Ellis et al, 2015). 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).…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2018

View full text Add to dashboard Cite

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.

show abstract

Hfq binds directly to the ribosome‐binding site of IS10 transposase mRNA to inhibit translation

Cited by 60 publications

References 66 publications

Alternative Hfq‐sRNA interaction modes dictate alternative mRNA recognition

Alternative Hfq‐sRNA interaction modes dictate alternative mRNA recognition

Hfq assists small RNAs in binding to the coding sequence of ompD mRNA and in rearranging its structure

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

Contact Info

Product

Resources

About