@article{EulalioFroehlichManoetal.2011,
  author    = {Eulalio, Ana and Fr{\"o}hlich, Kathrin S. and Mano, Miguel and Giacca, Mauro and Vogel, J{\"o}rg},
  title     = {A Candidate Approach Implicates the Secreted Salmonella Effector Protein SpvB in P-Body Disassembly},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-68928},
  year      = {2011},
  abstract  = {P-bodies are dynamic aggregates of RNA and proteins involved in several post-transcriptional regulation processes. Pbodies have been shown to play important roles in regulating viral infection, whereas their interplay with bacterial pathogens, specifically intracellular bacteria that extensively manipulate host cell pathways, remains unknown. Here, we report that Salmonella infection induces P-body disassembly in a cell type-specific manner, and independently of previously characterized pathways such as inhibition of host cell RNA synthesis or microRNA-mediated gene silencing. We show that the Salmonella-induced P-body disassembly depends on the activation of the SPI-2 encoded type 3 secretion system, and that the secreted effector protein SpvB plays a major role in this process. P-body disruption is also induced by the related pathogen, Shigella flexneri, arguing that this might be a new mechanism by which intracellular bacterial pathogens subvert host cell function.},
  subject      = {Salmonella},
  language  = {en}
}
@article{FroehlichPapenfortBergeretal.2012,
  author    = {Fr{\"o}hlich, Kathrin S. and Papenfort, Kai and Berger, Allison A. and Vogel, J{\"o}rg},
  title     = {A conserved RpoS-dependent small RNA controls the synthesis of major porin OmpD},
  series = {Nucleic Acids Research},
  volume    = {40},
  journal   = {Nucleic Acids Research},
  number    = {8},
  doi       = {10.1093/nar/gkr1156},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-134230},
  pages     = {3623-3640},
  year      = {2012},
  abstract  = {A remarkable feature of many small non-coding RNAs (sRNAs) of Escherichia coli and Salmonella is their accumulation in the stationary phase of bacterial growth. Several stress response regulators and sigma factors have been reported to direct the transcription of stationary phase-specific sRNAs, but a widely conserved sRNA gene that is controlled by the major stationary phase and stress sigma factor, Sigma(S) (RpoS), has remained elusive. We have studied in Salmonella the conserved SdsR sRNA, previously known as RyeB, one of the most abundant stationary phase-specific sRNAs in E. coli. Alignments of the sdsR promoter region and genetic analysis strongly suggest that this sRNA gene is selectively transcribed by Sigma(S). We show that SdsR down-regulates the synthesis of the major Salmonella porin OmpD by Hfq-dependent base pairing; SdsR thus represents the fourth sRNA to regulate this major outer membrane porin. Similar to the InvR, MicC and RybB sRNAs, SdsR recognizes the ompD mRNA in the coding sequence, suggesting that this mRNA may be primarily targeted downstream of the start codon. The SdsR-binding site in ompD was localized by 3'-RACE, an experimental approach that promises to be of use in predicting other sRNA-target interactions in bacteria.},
  language  = {en}
}
@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{FroehlichHanekePapenfortetal.2016,
  author    = {Fr{\"o}hlich, Kathrin S. and Haneke, Katharina and Papenfort, Kai and Vogel, J{\"o}rg},
  title     = {The target spectrum of SdsR small RNA in Salmonella},
  series = {Nucleic Acids Research},
  volume    = {44},
  journal   = {Nucleic Acids Research},
  number    = {21},
  doi       = {10.1093/nar/gkw632},
  url       = {http://nbn-resolving.de/urn:nbn:de:bvb:20-opus-175365},
  pages     = {10406-10422},
  year      = {2016},
  abstract  = {Model enteric bacteria such as Escherichia coli and Salmonella enterica express hundreds of small non-coding RNAs (sRNAs), targets for most of which are yet unknown. Some sRNAs are remarkably well conserved, indicating that they serve cellular functions that go beyond the necessities of a single species. One of these 'core sRNAs' of largely unknown function is the abundant ∼100-nucleotide SdsR sRNA which is transcribed by the general stress σ-factor, σ\(^{S}\) and accumulates in stationary phase. In Salmonella, SdsR was known to inhibit the synthesis of the species-specific porin, OmpD. However, sdsR genes are present in almost all enterobacterial genomes, suggesting that additional, conserved targets of this sRNA must exist. Here, we have combined SdsR pulse-expression with whole genome transcriptomics to discover 20 previously unknown candidate targets of SdsR which include mRNAs coding for physiologically important regulators such as the carbon utilization regulator, CRP, the nucleoid-associated chaperone, StpA and the antibiotic resistance transporter, TolC. Processing of SdsR by RNase E results in two cellular SdsR variants with distinct target spectra. While the overall physiological role of this orphan core sRNA remains to be fully understood, the new SdsR targets present valuable leads to determine sRNA functions in resting bacteria.},
  language  = {en}
}