Cooperativity between two transcription regulators occurs through protein-protein interactions with a general transcription factor complex and potentiates the parallel evolution of their DNA binding sites.
Combined light and electron microscopy reveals a new function for Arp2/3-mediated actin assembly in nuclear envelope rupture, which leads to a separation of nuclear membranes and pores from the lamina.
GCNA proteins comprise a previously unnoticed family of proteins that has been enriched in cells carrying a heritable genome since the invention of sexual reproduction in eukaryotes, and has had reproductive function for at least 600 million years.
The intrinsically disordered N-terminus of Sfr1 contains two Rad51 binding sites that facilitate Rad51 filament stabilization and ATPase stimulation by the Swi5-Sfr1 complex, leading to efficient Rad51-driven strand exchange.
Advanced microscopy techniques reveal that clusters of Pom1 kinase at the membrane represent the functional unit that shape the concentration gradients and modulate Pom1 mid-cell levels according to cell size.