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Differential eIF4E binding to transcription initiation nucleotides and alternative promoter usage of eIF1A, PABP and other genes are involved in the response of the translation machinery to energy stress.

Eukaryotic translation initiation factor 4A is stimulated by the ribosomal pre-initiation complex and promotes the recruitment of mRNAs regardless of their degree of structure.

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.

An ensemble of cryo-EM structures reveals how eukaryotic elongation factor 2 positions the first codon of a viral mRNA for translation.

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.

The retarding effect of a ribosome-bound internal ribosome entry site on eukaryotic protein synthesis is largely overcome following translocation of tripeptidyl-tRNA.

Specific amino acids in the N-terminus of the replication initiator protein DnaA inhibit translation elongation upon carbon starvation, illustrating that the identity of the N-terminal amino acids of a protein can modulate protein synthesis yield under changing conditions.

A model reveals how translation of an mRNA leader could provide resistance to global downregulation of translation.

The small subunit ribosomal protein uS7/Rps5 interacts with translation initiation factor eIF2α to stabilize first the open, and then the closed conformation of the pre-initiation complex to promote accurate start codon selection in vivo.