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.
Without ribosome recycling factor, ribosomes in Escherichia coli accumulate in 3'-UTRs and queue upstream of stop codons, but no effects were observed on the translational coupling of neighboring genes.
Utilizing a conserved mechanism, a ribosome can initiate translation from a site within the insulin receptor mRNA to maintain protein synthesis even when standard mechanisms of initiating translation have been inhibited by stress.
Although puromycin staining is often used to examine subcellular translation, puromycin-labeled proteins are rapidly released from ribosomes even in the presence of elongation inhibitors, which may confound translation site localization.
Eukaryotic translation elongation factor 1A1 controls the process of heat shock response, from transcriptional activation of the HSP70 gene, to HSP70 mRNA stabilization, nuclear export, and translation.