Ribosome production is unexpectedly integrated into innate cell-intrinsic responses that regulate double strand DNA-sensing and inflammatory cytokine induction in infected and uninfected cells.

Eukaryotic translation initiation factor 3 (eIF3) is required to stabilize the binding of mRNA at the exit channel of the small ribosomal subunit and acts at the entry channel to accelerate mRNA recruitment to the translation preinitiation complex.

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

Alkylation stress modify mRNAs and results in translation arrest, which activates the ribosome-rescue pathway of trans translation in bacteria.

The messenger RNA encoding La-related protein-4 (LARP4) contains a short region of instability whose codon clusters are sensitive to low abundance tRNAs that when elevated increase LARP4 activity for poly(A) lengthening of ribosomal protein mRNAs and other mRNAs.

Single-molecule observations reveal a mechanism that may be used by multiple competing regulatory proteins to control ribosomal RNA production during rapid bacterial cell growth.

Embryonic development requires autophagy-dependent degradation of ribosomal RNAs.

The size of the mRNA fragment protected by a ribosome depends on the ribosome's conformation, which enables studies of the distinct steps of decoding and translocation at single-codon resolution.

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

A critical component of the cellular response to unfolded proteins is the widespread rescue of ribosomes that stall on endonucleolytically-cleaved mRNA transcripts.