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.

Asc1/RACK1 promotes the translation of mRNAs associated with the translational closed loop complex, which have short open reading frames and encode proteins required for core metabolic processes.

A mutant impaired for ribosome recycling exhibits translational reprogramming wherein strong mRNAs outcompete weak mRNAs, also observed when preinitiation complexes are diminished by eIF2α phosphorylation or 40S ribosomal subunit depletion.

A structural element of mRNA exit channel protein Rps5 performs a critical role in start codon recognition during translation initiation by stabilizing initiator tRNA binding to the pre-initiation complex.

A new in vitro approach allows measurement of the efficiency of the early steps of translation initiation on every messenger RNA in yeast simultaneously.

Activation of the stress response pathway in young cells extends replicative lifespan, not by reducing global protein synthesis per se, but by Gcn4-mediated autophagy induction.

For poly(A)-tail length to influence mRNA translational efficiency, poly(A)-binding protein (PABPC) must be limiting, mRNAs lacking PABPC must be stable, and translation initiation must be sensitive to PABPC levels.

Most of the mRNAs whose translation is resistant to the stress-induced repression of protein synthesis contain upstream open reading frames that are efficiently translated under normal conditions.

BUD23 links ribosome function with mitochondrial protein expression and efficient oxidative phosphorylation by promoting selective mRNA translation and is therefore critical to mouse development and postnatal cardiac function.

The eIF3 translation initiation complex exerts specific regulation on neuronal protein levels by targeting mRNAs with GC-rich 5' UTR.