Highlights • Proteins begin to fold within the polypeptide exit tunnel of the ribosome. • Ribosomes
change the landscape of protein folding. • Ribosomes can stabilize non-native compact …

The ribosome is a molecular machine responsible for protein synthesis and a major target
for small-molecule inhibitors. Compared to the wealth of structural information available on …

Protein domains can fold into stable tertiary structures while they are synthesized on the
ribosome. We used a high-performance, reconstituted in vitro translation system to investigate …

As a model for brain inflammation we previously studied transcriptional profiles of tumor
necrosis factor-α (TNF)-treated U373 astroglioma cells. In previous work we were able to …

Elongation factor G ( EF ‐ G ) promotes the movement of two tRNA s and the mRNA through
the ribosome in each cycle of peptide elongation. During translocation, the tRNA s …

Nascent proteins emerging from translating ribosomes in bacteria are screened by a number
of ribosome-associated protein biogenesis factors, among them the chaperone trigger …

Ribosomes synthesizing inner membrane proteins in Escherichia coli are targeted to the
membrane by the signal recognition particle (SRP) pathway. By rapid kinetic analysis we show …

Elongation factor G (EF-G) is a GTPase that catalyzes tRNA and mRNA translocation during
the elongation cycle of protein synthesis. The GTP-bound state of the factor on the ribosome …

The translocation of tRNAs through the ribosome proceeds through numerous small steps in
which tRNAs gradually shift their positions on the small and large ribosomal subunits. The …

10.7554/eLife.34252.001 Release factors RF1 and RF2 promote hydrolysis of peptidyl-tRNA
during translation termination. The GTPase RF3 promotes recycling of RF1 and RF2. Using …