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The Sec pathway, which transports proteins across membranes, is ubiquitous and essential for viability in all three domains of life. At the core of the pathway is the translocase, a dynamic nanomachine that catalyses transmembrane crossing. This Review considers the latest data on the structure and function of the bacterial Sec translocase.
The long-held belief that bacteria rely solely on homologous recombination for the repair of double-strand breaks was recently overturned by evidence that many bacterial genera contain a system for non-homologous end joining (NHEJ). Biochemical, structural and genetic studies are beginning to define an NHEJ pathway that has distinctive features and enzymatic components.
The complex life cycle ofMyxococcus xanthusincludes predation, swarming, fruiting-body formation and sporulation. The large genome of this bacterium contains eight chemotaxis gene clusters that define eight two-component chemosensory pathways, most of which have dedicated functions in motility or development.
Every year there are an estimated 500,000 new cases of visceral leishmaniasis (VL) and more than 50,000 deaths from the disease, a death toll that is surpassed among the parasitic diseases only by malaria. The epidemiology, clinical presentation and pathogenesis of VL are reviewed, along with the current control strategies and research challenges.
The evidence suggests that a novel secretion system, which is unlike type I–VI secretion systems, exports proteins across the highly impermeable cell walls of mycobacterium. In this Opinion, Wilbert Bitter and colleagues propose to call this system, in line with the accepted nomenclature, type VII secretion.
Owing to their ability to couple ion movement with ATP hydrolysis or synthesis, F-type and V-type ATPases constitute the cornerstone of cellular bioenergetics and are present in all three domains of life. In this Opinion, Eugene Koonin and colleagues use sequence and structural data to develop an evolutionary scenario for these ubiquitous molecular machines.
