Computational and theoretical models reveal mechanisms by which protein compartments assemble around enzymes and reagents to facilitate reactions in bacteria, allowing the identification of strategies for reengineering such compartments as customizable nanoreactors.
A pathogen effector mimics starvation-induced autophagy by subverting host endomembrane trafficking to stimulate biogenesis of autophagosomes around pathogen feeding sites, revealing how pathogens interlock distinct host compartments to facilitate infection.
Structure of the Mrp antiporter, an ancestor of respiratory complex I, suggests a mechanism of coupling between cation and proton translocation, applicable to a large family of related membrane proteins.
The circadian clock of Synechococcus elongatus PCC7942 schedules the activity of the transcription factor RpaA, which controls key events in carbon metabolism that contribute to cell fitness in conditions mimicking the natural environment.
Physiological differentiation during symbiosis leads to division of labor between smaller and larger cells in an uncultured bacterial tubeworm symbiont population and results in remarkable metabolic diversity and complexity.
Low-field single-sided magnetic resonance diffusion methods detect and measure permeability of sub-micron compartments which likely include cell processes, organelles, and cellular vesicles within ex vivo mouse spinal cords.
Proteasomes are protected from autophagic elimination upon carbon starvation by sequestration into cytoplasmic storage granules, which aid cell fitness by providing a cache of proteasomes that can be rapidly remobilized when carbon availability improves.