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.
Interactions of eIF4A and eIF4E with specific amino-acids in the N-terminal domain of DEAD-box helicase Ded1 enhance bulk polysome assembly and translation of reporter mRNAs with structured leaders in vivo.
Yeast RNA helicase Ded1 stimulates ribosome recruitment of structure-laden native mRNAs in a reconstituted system by interactions between domains in Ded1 and initiation factor eIF4G that stabilizes a Ded1-eIF4F complex.
Substitutions in general translation initiation factor eIF1A found as recurring somatic mutations in uveal melanoma destabilize the closed conformation of the preinitiation complex at the start codon and increase discrimination against suboptimal initiation codons genome-wide.
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.
The hepatitis C virus IRES binds and remodels preassembled eukaryotic translation preinitiation complexes, using specific initiation factor protein within a "bacterial-like" mode of initiation that can function in both stressed and unstressed cells.
La-related protein 1 specifically and directly binds the 5' cap and first nucleotide of mRNAs encoding ribosomal proteins and translation factors, inhibiting the assembly of translation initiation factors on these messages and therefore their translation.