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.

Mathematical models reveal that under the physiologically different conditions ambient and high CO2, two algal microcompartments are metabolically connected by facilitated transport.

A peroxidase-containing nanocompartment in the bacterial pathogen Mycobacterium tuberculosis protects against oxidative stress and antibiotic treatment in the host.

A protein-bounded organelle-like compartment from Synechococcus elongatus PCC 7942 is upregulated under sulfur starvation and contains a cysteine desulfurase cargo enzyme.

A minimal cell-like system with defined geometry has been used to investigate the establishment and spatial control of a protein gradient that positions the bacterial cell division machinery.

Carboxysomes, the carbon-fixation machinery of cyanobacteria, are equidistantly-positioned by dynamic gradients of the protein McdA on the nucleoid that emerge through interaction with a previously unidentified carboxysome factor, McdB.

A novel B12 containing photoreceptor is synthesized as two different isoforms that interact with the same transcription factor, with one isoform directing activation and the other promoting repression of photosystem synthesis.

Carbon-fixing organelles, called carboxysomes, link to their spatial organization system in the bacterial cell by a hexameric protein that forms pH-dependent condensates via a nuanced multidomain mechanism.

A starvation-induced drop in cytosolic pH promotes assembly of budding yeast glutamine synthetase into enzymatically inactive filaments that function as enzyme storage depots.

In vitro, in vivo and in silico evidence suggests that bacteria exploit intrinsic chromosomal fluctuations to achieve intracellular transport.