Using bioinformatic and biochemical approaches, the study has explained the discriminator base anomaly in bacterial tRNA(Gly) through identification of the key determinant of DTD specificity.

Translation quality control protects the cell from environmental stresses that could potentially lead to the toxic accumulation of non-proteinogenic amino acids in the proteome.

Identification of a two-tier functional redundancy to combat proteostasis imbalance induced due to tRNA expansion and oxidative stress in multicellular animals.

The Bi-Genomic Mitochondrial-Split-GFP, where both fragments of the Split-GFP are expressed by separated translation machineries, shuts off cytosolic fluorescence of dual-localized proteins, allowing visualization of their mitochondrial echoforms.

Cryo-EM structures of 70S•RelA ribosome complexes reveal how cognate deacyl-tRNA activates RelA.

Structural biology has elucidated the mechanism of a configuration-specific enzyme that decouples D-amino acids from the translational machinery and, therefore, is involved in the enforcement of homochirality during protein synthesis.

An ancient complex comprising the eukaryotic elongation factor-1A and aminoacylated tRNA is shown to be the target of a cyclic heptapeptide and two unrelated natural products with potent anticancer activity.

Genetic, biochemical, and bioinformatic analyses reveal how expanding metabolic repertoire interferes with fundamental processes like protein synthesis inside cells and the role of D-aminoacyl-tRNA deacylase2 in protecting these processes during terrestrialisation.

Microbial cells optimally structure their proteomes in order to mutually maximize metabolism and translation, as established by an extensive comparison between data and a low-dimensional model of cellular physiology.

A time-resolved analysis of protein and RNA concentrations and interactions during proteostasis stress highlights the dominant role of translation regulation and a shift of energy metabolism.