The retarding effect of a ribosome-bound internal ribosome entry site on eukaryotic protein synthesis is largely overcome following translocation of tripeptidyl-tRNA.

‘Optical tweezers’ measurements of single ribosomes and single mRNA molecules show that the translation rate depends exponentially on the applied force, and suggests that the ribosome functions as a Brownian ratchet.

Quantification of all the major on- and off-pathway kinetic parameters in the transcription elongation cycle reveals that RNA polymerase II translocates slowly in a linear, non-branched Brownian ratchet mechanism.

A complex that catalyzes the membrane integration of β barrel proteins and a molecular chaperone promote the complete assembly of a bacterial virulence factor in vitro.

The rate of DNA unwinding by RecQ helicases is dramatically modulated by the DNA duplex stability in a geometry-dependent manner, providing an intrinsic mechanism for suppressing illegitimate recombination.

Cyclic peptide natural products didemnin B and ternatin-4 bind the same hydrophobic pocket of eEF1A to inhibit mRNA translation but exhibit kinetic differences that influence rate-limiting conformational changes underpinning aminoacyl-tRNA selection.

The time it takes to secrete a protein is dominated by diffusion of positively charged arginines through the channel across the membrane, but lysines avoid this problem as they are neutralised before transport.

A model reveals how translation of an mRNA leader could provide resistance to global downregulation of translation.

Genome dilution limits cell growth by modulating the activities, rather than the concentrations, of RNA polymerases and ribosomes, and is accompanied by changes in proteome composition.

In neuronal mitophagy, Parkin and OPTN induce efficient sequestration of damaged somal mitochondria into autophagosomes, but slow turnover via lysosomal acidification may be a point of vulnerability for the cell.