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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.

Mutually exclusive RNA secondary structures regulate translation initiation of DinQ in Escherichia coli