@article{DimastrogiovanniFroehlichBandyraetal.2014,
  author    = {Dimastrogiovanni, Daniela and Fr{\"o}hlich, Kathrin S. and Bandyra, Katarzyna J. and Bruce, Heather A. and Hohensee, Susann and Vogel, J{\"o}rg and Luisi, Ben F.},
  title     = {Recognition of the small regulatory RNA RydC by the bacterial Hfq protein},
  series = {eLife},
  volume    = {3},
  journal   = {eLife},
  number    = {e05375},
  issn      = {2050-084X},
  doi       = {10.7554/eLife.05375},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-114191},
  year      = {2014},
  abstract  = {Bacterial small RNAs (sRNAs) are key elements of regulatory networks that modulate gene expression. The sRNA RydC of Salmonella sp. and Escherichia coli is an example of this class of riboregulators. Like many other sRNAs, RydC bears a 'seed' region that recognises specific transcripts through base-pairing, and its activities are facilitated by the RNA chaperone Hfq. The crystal structure of RydC in complex with E. coli Hfq at 3.48 angstrom resolution illuminates how the protein interacts with and presents the sRNA for target recognition. Consolidating the protein-RNA complex is a host of distributed interactions mediated by the natively unstructured termini of Hfq. Based on the structure and other data, we propose a model for a dynamic effector complex comprising Hfq, small RNA, and the cognate mRNA target.},
  language  = {en}
}
@article{BandyraSaidPfeifferetal.2012,
  author    = {Bandyra, Katarzyna J. and Said, Nelly and Pfeiffer, Verena and G{\´o}rna, Maria W. and Vogel, J{\"o}rg and Luisi, Ben F.},
  title     = {The Seed Region of a Small RNA Drives the Controlled Destruction of the Target mRNA by the Endoribonuclease RNase E},
  series = {Molecular Cell},
  volume    = {47},
  journal   = {Molecular Cell},
  number    = {6},
  doi       = {10.1016/j.molcel.2012.07.015},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-126202},
  pages     = {943-953},
  year      = {2012},
  abstract  = {Numerous small non-coding RNAs (sRNAs) in bacteria modulate rates of translation initiation and degradation of target mRNAs, which they recognize through base-pairing facilitated by the RNA chaperone Hfq. Recent evidence indicates that the ternary complex of Hfq, sRNA and mRNA guides endoribonuclease RNase E to initiate turnover of both the RNAs. We show that a sRNA not only guides RNase E to a defined site in a target RNA, but also allosterically activates the enzyme by presenting a monophosphate group at the 5′-end of the cognate-pairing "seed." Moreover, in the absence of the target the 5′-monophosphate makes the sRNA seed region vulnerable to an attack by RNase E against which Hfq confers no protection. These results suggest that the chemical signature and pairing status of the sRNA seed region may help to both 'proofread' recognition and activate mRNA cleavage, as part of a dynamic process involving cooperation of RNA, Hfq and RNase E.},
  language  = {en}
}