title: Mutually exclusive RNA secondary structures regulate translation initiation of DinQ in Escherichia coli.
abstract: Protein translation can be affected by changes in the secondary structure of mRNA. The dinQ gene in Escherichia coli encodes a primary transcript (+1) that is inert to translation. Ribonucleolytic removal of the 44 first nucleotides converts the +1 transcript into a translationally active form, but the mechanism behind this structural change is unknown. Here we present experimental evidence for a mechanism where alternative RNA secondary structures in the two dinQ mRNA variants affect translation initiation by mediating opening or closing of the ribosome binding sequence. This structural switch is determined by alternative interactions of four sequence elements within the dinQ mRNA and also by the agrB antisense RNA. Additionally, the structural conformation of +1 dinQ suggests a locking mechanism comprised of an RNA stem that both stabilizes and prevents translation initiation from the full-length dinQ transcript. BLAST search and multiple sequence alignments define a new family of dinQ-like genes widespread in Enterobacteriaceae with close RNA sequence similarities in their 5' untranslated regions. Thus, it appears that a whole new family of genes is regulated by the same mechanism of alternative secondary RNA structures.
authors.affiliation: Department of Microbiology, University of Oslo and Oslo University Hospital, Rikshospitalet, N-0424 Oslo, Norway.
authors.forename: Knut I
authors.initials: KI
authors.lastname: Kristiansen
authors.affiliation: Department of Microbiology, University of Oslo and Oslo University Hospital, Rikshospitalet, N-0424 Oslo, Norway.
authors.forename: Ragnhild
authors.initials: R
authors.lastname: Weel-Sneve
authors.affiliation: Department of Microbiology, University of Oslo and Oslo University Hospital, Rikshospitalet, N-0424 Oslo, Norway.
authors.forename: James A
authors.initials: JA
authors.lastname: Booth
authors.affiliation: Department of Microbiology, University of Oslo and Oslo University Hospital, Rikshospitalet, N-0424 Oslo, Norway.|Department of Cancer Research and Molecular Medicine, Norwegian University of Science and Technology, N-7491 Trondheim, Norway.
authors.forename: Magnar
authors.initials: M
authors.lastname: Bjørås
mesh_terms: D020121:5' Untranslated Regions; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000235:genetics*; D008565:Membrane Proteins / Q000235:genetics*; D009690:Nucleic Acid Conformation; D014176:Protein Biosynthesis; D020871:RNA Stability; D012329:RNA, Bacterial / Q000737:chemistry / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D020121:5' Untranslated Regions; C581618:DinQ protein, E coli; D029968:Escherichia coli Proteins; D008565:Membrane Proteins; D012329:RNA, Bacterial
keywords: DinQ; E. coli; RNA processing; RNA structure; translation initiation