Eukaryotic translation initiation factor 3 (eIF3) is required to stabilize the binding of mRNA at the exit channel of the small ribosomal subunit and acts at the entry channel to accelerate mRNA recruitment to the translation preinitiation complex.
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.
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.
Phosphorylated translation initiation factor eIF2, a potent inhibitor of protein synthesis in eukaryotic cells, is also inhibitory to protein synthesis when bound to GTP and initiator tRNA broadening the reach and immediacy of eIF2-mediated control.
The essential mycobacterial transcription factor RbpA interacts with promoter DNA and cooperates with another essential transcription factor, CarD, to stimulate the formation of an intermediate leading to the open promoter complex.
The cyclic-peptide antibiotic GE23077 inhibits bacterial RNA polymerase through a novel target that exhibits low susceptibility to target-based resistance and that enables synthesis of bipartite inhibitors that are exceptionally potent and refractory to target-based resistance.
Structures of RNA polymerase I transcription machinery revealed a ratcheting motion within the complex in coordination with three distinct functional states, implicating a novel mechanism for promoter bubble opening in the absence of ATP hydrolysis.