Dr Mark Glover
Department of Biochemistry, University of Alberta, Edmonton, Canada
The FinO family of RNA chaperones regulate sRNA function throughout gram negative bacteria. Many of the best characterized family members bind to rho-independent transcription termination structures at the 3’ ends of sRNAs and mediate pairing of the sRNA with their mRNA targets. The crystal structure of the FinO domain of the Legionella pneumophila chaperone RocC bound to its sRNA target reveals a novel interaction that recognizes both the stem and the 3’ end of the terminator structure. The structure suggests a mechanism by which different FinO proteins can selectively bind RNAs with different 3’ tail lengths, which is likely conserved throughout the FinO family. Biochemical and in vivo studies indicate that intrinsically disordered regions adjacent to the FinO domain are also essential for sRNA regulation, by remodeling RNA structure to facilitate RNA-RNA association.