Antoine M. van Oijen

TL;DR: This review will discuss single-molecule studies of the replisome, the protein complex responsible for the coordinated replication of double-stranded DNA, and will focus on new insights obtained into the dynamic nature of the composition of the DNA-replication machinery and how the dynamic replacement of components plays a role in the regulation of theDNA-replications process.

TL;DR: Single-molecule fluorescence imaging is used to quantify the kinetic signatures of interactions of UvrA with Mfd and UvrB in live cells to illustrate a non-perturbative, imaging-based approach to quantify the kinetic signature of damage recognition enzymes participating in multiple pathways in cells.

TL;DR: Effects of mutations in HA indicate that withdrawal of the fusion peptide from a pocket in the pre-fusion trimer is rate-limiting for both events, but the requirement for cooperative action of several HAs to bring the fusing membranes together leads to a long-lived intermediate state for single, extended HA trimers.

TL;DR: It is demonstrated that the binding energy for CHD4-nucleosome complex formation—even in the absence of nucleotide—triggers significant conformational changes in DNA at the entry side, effectively priming the system for remodelling.