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Arluison, Vé,ronique,Hohng, Sungchul,Roy, Rahul,Pellegrini, Olivier,Ré,gnier, Philippe,Ha, Taekjip Oxford University Press 2007 Nucleic acids research Vol.35 No.3
<P>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, <I>rpoS</I>. 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 <I>rpoS</I> 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 <I>rpoS</I> and by aiding in the slow disruption of the <I>rpoS</I> secondary structure. Unexpectedly, Hfq also disrupts a preformed complex between <I>rpoS</I> and DsrA. While it may not be a frequent event <I>in vivo</I>, 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 <I>rpoS</I> but also possesses RNA chaperoning properties that facilitates dynamic RNA–RNA interactions.</P>