A new optical tweezers assay sheds light on the mechanism of cooperation and force generation by the subunits of RecBCD, critical for the repair of double strand breaks in bacteria.

Deep penetration and transmission of mechanical force to regulate ER functions depends on not only the passive cytoskeletal support, but also the active actomyosin contractility, which is dispensable for mechanotransduction at the plasma membrane.

Sec1/Munc18-family proteins chaperone SNARE assembly via a common templating mechanism.

‘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.

Single-molecule methods reveal that cytidine triphosphate promotes DNA condensation specifically at bacterial centromeres by facilitating one-dimensional diffusion of ParB from parS sites.

The Munc18-1 protein promotes formation of the t-SNARE complex and the half-zippered SNARE complex, two rate-limiting steps of SNARE assembly, to enhance membrane fusion.

In vitro single-particle tracking reveals that ATP binding increases the one-dimensional diffusion of yeast chromatin remodeler SWR1 on DNA stretched between optical tweezers and diffusion is confined by protein roadblocks and nucleosomes.

Single-particle imaging of RSC and ISW2 chromatin remodelers on DNA stretched between dual optical tweezers reveals distinctive 1D diffusion and opposing push–pull nucleosome translocation on engagement with sparse nucleosome arrays.

The energy landscape of SNARE folding and assembly is optimized for efficient stage-wise membrane fusion.

An exceedingly low speed limit was estimated for a helical hairpin formation by analyzing hours-long, incessant structural transitions.