This blog post comments on the results published by Fujiwara and co-workers in the 2020 Cell Reports article “Proteome-wide capture of co-translational protein dynamics in Bacillus subtilis using TnDR, a transposable protein-dynamics reporter.”

The study of mechanical force generation and its influence on biological systems has expanded in recent years. In the realm of nascent protein folding, we now know that both unstructured and folded nascent proteins generate forces on the order of piconewtons that propagate down the nascent chain. These forces can distort the functional site of the ribosome and may influence the rate of translation (PMIDs: 30824598, 29577725). It has also been shown that translational arrest can be relieved by mechanical force (PMID: 25908824). Much study has focused on so-called arrest peptides, short peptide sequences that interact so strongly with the ribosome exit tunnel that they can completely stall translation (e.g., SecM, MifM).