Translation pauses occur in strategic positions to facilitate the production of properly folded membrane proteins in bacteria.

E. coli ribosomes incapable of base-pairing with the Shine-Dalgarno sequence are still selective for annotated start sites, indicating these sites are hard-wired for initiation by other mRNA features.

Cryo-EM structures of the 30S*RNAP complex visualize co-localization of the transcription and translation machineries and provide insights into the transcription-translation synchrony, which coordinates gene expression in bacteria.

With the removal of confounding artifacts, ribosome profiling can yield insight into the mechanism of protein synthesis in bacteria at high resolution.

Thousands of novel open-reading frames (ORFs) are translated in the bacterium Mycobacterium tuberculosis, including many short ORFs that are likely to contribute to cell fitness.

Operonic mRNAs in bacteria are comprised of ORF (open reading frame)-wide units of secondary structure, which are intrinsically distinct between adjacent ORFs and encode a rough blueprint for ORF-specific translation efficiency.

Ensemble cryo-EM visualizes how structural rearrangements poise the newly made protein and release factor RF2 to dissociate in preparation for ribosome recycling.

A new biochemical method tests whether or not the pre-existing RNA structural correlations couple small molecule binding to gene expression in a paradigmatic riboswitch.

A genetic selection of toxicity suppressors coupled to high-throughput sequencing has captured metastable RNA structures that co-transcriptionally inhibit the translation of a bacterial toxin.