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

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

Two integrated approaches shed light on how XBP1 arrest peptide induces intermediate level of translational pausing and identify hotspot positions to make it stronger.

Biochemical and genome-wide analysis demonstrates that m¹G37 is important for tRNA aminoacylation and for the entire elongation cycle of protein synthesis.

Biofilm formation by Bacillus subtilis relies on a sensing mechanism for the amino acid serine that does not depend on a dedicated protein or RNA.

By sterically hindering tRNA binding and inhibiting translation elongation, mRNA stem-loops can modulate gene expression.

The translational GTPase GTPBP1 prevents ribosome stalling during tRNA deficiency and is necessary for neuronal survival.

Adaptations in protein synthesis and mRNA surveillance machinery enabled the malaria-causing parasite P. falciparum to efficiently and accurately translate long polyA nucleotide runs into long poly-lysine peptides.

Ribosomes undergo an unanticipated movement (‘sliding’) while translating homopolymeric A sequences, which provides a biochemical rationale for the observation that iterated AAA codons are under-represented in gene-coding sequences.

The yeast mRNA decapping enzyme Dcp1/Dcp2 repressses many genes whose products are required on poor carbon or nitrogen sources in nutrient-replete cells by mRNA decapping and degradation or translational repression, adding post-transcriptional controls to the transcriptional repression of these functions.