Interactions of ribosomal protein S1 with DsrA and rpoS mRNA

Koleva, Rositsa I.; Austin, Christina A.; Kowaleski, Jeffrey M.; Neems, Daniel; Wang, Leyi; Vary, Calvin P.H.; Schlax, Paula J.

doi:10.1016/j.bbrc.2006.07.102

Cited by 15 publications

(17 citation statements)

References 43 publications

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“…Nevertheless, Hfq binding does not seem to be necessary for the interaction of rpoS and DsrA with 30S [125]. The same group showed using photochemical crosslinking that the r-protein S1 interacts with both RNAs on the 30S [126] and suggested that S1 might play a role in facilitating translation of sRNA regulated mRNAs.…”

Section: Dsra/rpos Translation Activationmentioning

confidence: 89%

Multiple ways to regulate translation initiation in bacteria: Mechanisms, regulatory circuits, dynamics

et al. 2015

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Section: Dsra/rpos Translation Activationmentioning

confidence: 89%

Multiple ways to regulate translation initiation in bacteria: Mechanisms, regulatory circuits, dynamics

et al. 2015

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“…At this temperature, the protein could promote these annealing and melting reactions only 30–75 times per generation time of the bacteria; therefore, some additional co-factors might also be involved in one or both of these Hfq activities in vivo . For example, ribosomal protein S1 has been already shown to bind to DsrA and rpoS (36) and was suggested to interact with Hfq and RNA polymerase (37). This also raises an interesting possibility of a coupling between transcription and Hfq-mediated translational regulation.…”

Section: Discussionmentioning

confidence: 99%

Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA

Arluison

Hohng

Roy

et al. 2007

Nucleic Acids Research

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Hfq protein is vital for the function of many non-coding small (s)RNAs in bacteria but the mechanism by which Hfq facilitates the function of sRNA is still debated. We developed a fluorescence resonance energy transfer assay to probe how Hfq modulates the interaction between a sRNA, DsrA, and its regulatory target mRNA, rpoS. The relevant RNA fragments were labelled so that changes in intra- and intermolecular RNA structures can be monitored in real time. Our data show that Hfq promotes the strand exchange reaction in which the internal structure of rpoS is replaced by pairing with DsrA such that the Shine-Dalgarno sequence of the mRNA becomes exposed. Hfq appears to carry out strand exchange by inducing rapid association of DsrA and a premelted rpoS and by aiding in the slow disruption of the rpoS secondary structure. Unexpectedly, Hfq also disrupts a preformed complex between rpoS and DsrA. While it may not be a frequent event in vivo, this melting activity may have implications in the reversal of sRNA-based regulation. Overall, our data suggests that Hfq not only promotes strand exchange by binding rapidly to both DsrA and rpoS but also possesses RNA chaperoning properties that facilitates dynamic RNA–RNA interactions.

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“…Because S1 is capable of binding to sRNAs with the same affinity as Hfq, it has been suggested that S1 can theoretically regulate sRNA stability as well. However, the biological relevance of this suggestion still needs to be elucidated (Koleva et al, 2006; Windbichler et al, 2008). …”

Section: Different Rna-binding Proteins That Act Post-transcriptionalmentioning

confidence: 99%

RNA-binding proteins involved in post-transcriptional regulation in bacteria

et al. 2015

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Post-transcriptional regulation is a very important mechanism to control gene expression in changing environments. In the past decade, a lot of interest has been directed toward the role of small RNAs (sRNAs) in bacterial post-transcriptional regulation. However, sRNAs are not the only molecules controlling gene expression at this level, RNA-binding proteins (RBPs) play an important role as well. CsrA and Hfq are the two best studied bacterial proteins of this type, but recently, additional proteins involved in post-transcriptional control have been identified. This review focuses on the general working mechanisms of post-transcriptionally active RBPs, which include (i) adaptation of the susceptibility of mRNAs and sRNAs to RNases, (ii) modulating the accessibility of the ribosome binding site of mRNAs, (iii) recruiting and assisting in the interaction of mRNAs with other molecules and (iv) regulating transcription terminator/antiterminator formation, and gives an overview of both the well-studied and the newly identified proteins that are involved in post-transcriptional regulatory processes. Additionally, the post-transcriptional mechanisms by which the expression or the activity of these proteins is regulated, are described. For many of the newly identified proteins, however, mechanistic questions remain. Most likely, more post-transcriptionally active proteins will be identified in the future.

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Interactions of ribosomal protein S1 with DsrA and rpoS mRNA

Cited by 15 publications

References 43 publications

Multiple ways to regulate translation initiation in bacteria: Mechanisms, regulatory circuits, dynamics

Multiple ways to regulate translation initiation in bacteria: Mechanisms, regulatory circuits, dynamics

Spectroscopic observation of RNA chaperone activities of Hfq in post-transcriptional regulation by a small non-coding RNA

RNA-binding proteins involved in post-transcriptional regulation in bacteria

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