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.

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

How the process of protein folding may be controlled by the Sec machinery to assist protein transport across membranes.

Evidence is presented that supports a completely new, diffusion-driven mechanism for transporting proteins across membranes in bacteria.

Mitochondria can tune the protein synthesis of nuclear-encoded proteins through condition-dependent mRNA localization that is regulated by translation elongation and the geometric constraints of the cell.

The unspliced HAC1 mRNA does not give rise to detectable protein in budding yeast, despite its cytoplasmic localization, due to a two-part post-transcriptional silencing mechanism.

The heme and HRI-mediated eIF2aP–ATF4 integrated stress response in erythropoiesis has a major global impact, especially under the stress condition of iron deficiency.

Two domains of the peripheral membrane protein Tim44 interact with two different sectors of a translocase to coordinate the translocation of proteins across the inner mitochondrial membrane.

Ire1α co-opts the Sec61 translocon channel to efficiently cleave its mRNA substrates during endoplasmic reticulum stress conditions.

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