Intermembrane crosstalk drives inner-membrane protein organization in Escherichia coli.

Gram-negative bacteria depend on energised protein complexes that connect the two membranes of the cell envelope. However, β-barrel outer-membrane proteins (OMPs) and α-helical inner-membrane proteins (IMPs) display quite different organisation. OMPs cluster into islands that restrict their lateral mobility, while IMPs generally diffuse throughout the cell.

Uncertainty assessment method for the Cs-137 fallout inventory and penetration depth.

Within the presented study, soil samples were collected in year 2007 at 20 different locations of the Greek terrain, both from the surface and also from depths down to 26 cm. Sampling locations were selected primarily from areas where high levels of Cs deposition after the Chernobyl accident had already been identified by the Nuclear Engineering Laboratory of the National Technical University of Athens during and after the year of 1986. At one location of relatively higher deposition, soil core samples were collected following a 60 m by 60 m Cartesian grid with a 20 m node-to-node distance.

The uronic acid content of coccolith-associated polysaccharides provides insight into coccolithogenesis and past climate.

Unicellular phytoplanktonic algae (coccolithophores) are among the most prolific producers of calcium carbonate on the planet, with a production of ∼10 coccoliths per year. During their lith formation, coccolithophores mainly employ coccolith-associated polysaccharides (CAPs) for the regulation of crystal nucleation and growth. These macromolecules interact with the intracellular calcifying compartment (coccolith vesicle) through the charged carboxyl groups of their uronic acid residues.

Structure and function of the Escherichia coli Tol-Pal stator protein TolR.

TolR is a 15-kDa inner membrane protein subunit of the Tol-Pal complex in Gram-negative bacteria, and its function is poorly understood. Tol-Pal is recruited to cell division sites where it is involved in maintaining the integrity of the outer membrane. TolR is related to MotB, the peptidoglycan (PG)-binding stator protein from the flagellum, suggesting it might serve a similar role in Tol-Pal.